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Conserved domains on  [gi|2462591655|ref|XP_054203386|]
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receptor-type tyrosine-protein phosphatase gamma isoform X3 [Homo sapiens]

Protein Classification

fibronectin type III domain-containing protein( domain architecture ID 12931095)

fibronectin type III (FN3) domain-containing protein may be involved in specific interactions with other molecules through its FN3 domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 859-1132 0e+00

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG has four splicing isoforms: three transmembrane isoforms, PTPRG-A, B, and C, and one secretory isoform, PTPRG-S, which are expressed in many tissues including the brain. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


:

Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 635.92  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  859 FSEDFEEVQRCTADMNITAEHSNHPENKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 938
Cdd:cd17667      1 FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  939 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKG 1018
Cdd:cd17667     81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1019 NPKGRQNERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 1098
Cdd:cd17667    161 NPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 240

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2462591655 1099 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 1132
Cdd:cd17667    241 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1216-1420 8.87e-158

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


:

Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 474.17  E-value: 8.87e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFVYWPSREESMNCEAFTVTLISKDR 1295
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNCEAFTVTLISKDR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1296 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGMLCAL 1375
Cdd:cd17670     81 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEFGAVSAGTLCAL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2462591655 1376 TTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAMLS 1420
Cdd:cd17670    161 TTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 67-359 3.70e-115

Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related proteins (CARPs) are sequence similar to carbonic anhydrases. Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism. CARPs have lost conserved histidines involved in zinc binding and consequently their catalytic activity. This sub-family of carbonic anhydrase-related domains found in tyrosine phosphatase receptors may play a role in cell adhesion.


:

Pssm-ID: 239396 [Multi-domain]  Cd Length: 253  Bit Score: 362.06  E-value: 3.70e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   67 GPEHWVTSSVSCG-GRHQSPIDILDQYARVGEEYQELQLDGFDNESsNKTWMKNTGKTVAILLKD---DYFVSGAGLPGR 142
Cdd:cd03122      1 NPKHWAKKYPACGeGRQQSPIDIVEDTQVQRQGLQPLHFDGYEELT-ASTTLENTGKTVILRLEGnssDPFVSGGPLLGR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  143 FKAEKVEFHWGHSNgSAGSEHSINGRRFPVEaedacrgdimlmlsqgmrfillglkkeqfeerkswttyqsMQIFFYNPD 222
Cdd:cd03122     80 YKFSEITFHWGTCN-SDGSEHSIDGHKFPLE----------------------------------------MQILHRNTD 118

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  223 DFDSFqTAISENRIIGAMAIFFQVSPRDNSALDPIIHGLKGVVHHEKETFLDPFVLRDLLPASLGSYYRYTGSLTTPPCS 302
Cdd:cd03122    119 FFDSF-EAIKSPGGVLALAYLFELSHEDNPFLDPIIEGLRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCS 197

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462591655  303 EIVEWIVFRRPVPISYHQLEAFYSIFTTEQQDhVKSVEYLRNNFRPQQRLHDRVVSK 359
Cdd:cd03122    198 ETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGDYLPNNGRPQQPLGSRTVFS 253
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 388-478 3.83e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 55.20  E-value: 3.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  388 SPPIHMKVQPLNQTALQVSWSQPETIyHPPIMNYMISYSWTKNEDEKEktFTKDSDKDLKATISHVSPDSLYLFRVQAVc 467
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEDD-GGPITGYVVEYREKGSGDWKE--VEVTPGSETSYTLTGLKPGTEYEFRVRAV- 77

                           90
                   ....*....|.
gi 2462591655  468 RNDMRSDFSQT 478
Cdd:cd00063     78 NGGGESPPSES 88
PHA03169 super family cl27451
hypothetical protein; Provisional
 584-742 7.88e-06

hypothetical protein; Provisional


The actual alignment was detected with superfamily member PHA03169:

Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 49.97  E-value: 7.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  584 ASKQAARPVLATTealASPGPDGDSSPtkDGEGTEEGEKDEKSESEDGEREHEEDGEKDSEKKEKSGVTHAAEERNQtEP 663
Cdd:PHA03169   105 PSPSGSAEELASG---LSPENTSGSSP--ESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPE-EP 178

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591655  664 SPTPSSPNRTAEGGHQTIPGHEQDHTAVPTDQTGgrRDAGPGldPDMVTSTQVPPTATEEQYAgSDPKRPEMPSKKPMS 742
Cdd:PHA03169   179 EPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPG--EPQSPT--PQQAPSPNTQQAVEHEDEP-TEPEREGPPFPGHRS 252
 
Name Accession Description Interval E-value
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 859-1132 0e+00

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG has four splicing isoforms: three transmembrane isoforms, PTPRG-A, B, and C, and one secretory isoform, PTPRG-S, which are expressed in many tissues including the brain. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 635.92  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  859 FSEDFEEVQRCTADMNITAEHSNHPENKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 938
Cdd:cd17667      1 FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  939 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKG 1018
Cdd:cd17667     81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1019 NPKGRQNERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 1098
Cdd:cd17667    161 NPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 240

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2462591655 1099 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 1132
Cdd:cd17667    241 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1216-1420 8.87e-158

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 474.17  E-value: 8.87e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFVYWPSREESMNCEAFTVTLISKDR 1295
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNCEAFTVTLISKDR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1296 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGMLCAL 1375
Cdd:cd17670     81 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEFGAVSAGTLCAL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2462591655 1376 TTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAMLS 1420
Cdd:cd17670    161 TTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
858-1129 2.13e-119

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 373.92  E-value: 2.13e-119
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   858 GFSEDFEEVQRCTADMnITAEHSNHPENKHKNRYINILAYDHSRVKLRPLPGKDSkhsDYINANYVDGYNKAKAYIATQG 937
Cdd:smart00194    1 GLEEEFEKLDRLKPDD-ESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGS---DYINASYIDGPNGPKAYIATQG 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   938 PLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE--EYGNIIVTLKSTKIHACYTVRRFSIRNTkvkkg 1015
Cdd:smart00194   77 PLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNT----- 151

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  1016 qkgnpkGRQNERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKS 1095
Cdd:smart00194  152 ------GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK 225

                           250       260       270
                    ....*....|....*....|....*....|....
gi 2462591655  1096 TVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1129
Cdd:smart00194  226 EVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 67-359 3.70e-115

Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related proteins (CARPs) are sequence similar to carbonic anhydrases. Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism. CARPs have lost conserved histidines involved in zinc binding and consequently their catalytic activity. This sub-family of carbonic anhydrase-related domains found in tyrosine phosphatase receptors may play a role in cell adhesion.


Pssm-ID: 239396 [Multi-domain]  Cd Length: 253  Bit Score: 362.06  E-value: 3.70e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   67 GPEHWVTSSVSCG-GRHQSPIDILDQYARVGEEYQELQLDGFDNESsNKTWMKNTGKTVAILLKD---DYFVSGAGLPGR 142
Cdd:cd03122      1 NPKHWAKKYPACGeGRQQSPIDIVEDTQVQRQGLQPLHFDGYEELT-ASTTLENTGKTVILRLEGnssDPFVSGGPLLGR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  143 FKAEKVEFHWGHSNgSAGSEHSINGRRFPVEaedacrgdimlmlsqgmrfillglkkeqfeerkswttyqsMQIFFYNPD 222
Cdd:cd03122     80 YKFSEITFHWGTCN-SDGSEHSIDGHKFPLE----------------------------------------MQILHRNTD 118

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  223 DFDSFqTAISENRIIGAMAIFFQVSPRDNSALDPIIHGLKGVVHHEKETFLDPFVLRDLLPASLGSYYRYTGSLTTPPCS 302
Cdd:cd03122    119 FFDSF-EAIKSPGGVLALAYLFELSHEDNPFLDPIIEGLRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCS 197

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462591655  303 EIVEWIVFRRPVPISYHQLEAFYSIFTTEQQDhVKSVEYLRNNFRPQQRLHDRVVSK 359
Cdd:cd03122    198 ETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGDYLPNNGRPQQPLGSRTVFS 253
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
885-1129 6.99e-112

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 352.31  E-value: 6.99e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  885 NKHKNRYINILAYDHSRVKLRPLPGkdskHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNL 964
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG----PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  965 VEKGRRKCDQYWPTEN--SEEYGNIIVTLKSTKIH-ACYTVRRFSIRNTKVKKgqkgnpkgrqnERVVIQYHYTQWPDMG 1041
Cdd:pfam00102   77 EEKGREKCAQYWPEEEgeSLEYGDFTVTLKKEKEDeKDYTVRTLEVSNGGSEE-----------TRTVKHFHYTGWPDHG 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1042 VPEYALPVLTFVRR-SSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQY 1120
Cdd:pfam00102  146 VPESPNSLLDLLRKvRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQY 225


                   ....*....
gi 2462591655 1121 IFIHDALLE 1129
Cdd:pfam00102  226 IFLYDAILE 234
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
 60-356 3.86e-90

Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse the reversible hydration of carbon dioxide to bicarbonate.. CAs have essential roles in facilitating the transport of carbon dioxide and protons in the intracellular space, across biological membranes and in the layers of the extracellular space; they are also involved in many other processes, from respiration and photosynthesis in eukaryotes to cyanate degradation in prokaryotes. There are five known evolutionarily distinct CA families (alpha, beta, gamma, delta and epsilon) that have no significant sequence identity and have structurally distinct overall folds. Some CAs are membrane-bound, while others act in the cytosol; there are several related proteins that lack enzymatic activity. The active site of alpha-CAs is well described, consisting of a zinc ion coordinated through 3 histidine residues and a water molecule/hydroxide ion that acts as a potent nucleophile. The enzyme employs a two-step mechanism: in the first step, there is a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide; in the second step, the active site is regenerated by the ionisation of the zinc-bound water molecule and the removal of a proton from the active site. Beta- and gamma-CAs also employ a zinc hydroxide mechanism, although at least some beta-class enzymes do not have water directly coordinated to the metal ion.


Pssm-ID: 215000 [Multi-domain]  Cd Length: 247  Bit Score: 292.30  E-value: 3.86e-90
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655    60 WAYSGAYGPEHWVTSS-VSCGGRHQSPIDILDQYARVGEEYQELQldgFDNESSNKTWMKNTGKTVAILLKDD-YFVSGA 137
Cdd:smart01057    1 WGYEGKNGPEHWGKLDpPFCGGKRQSPIDIVTAEAQYDPSLKPLK---LSYDQPTAKRILNNGHTVQVNFDDDgSTLSGG 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   138 GLPGRFKAEKVEFHWGhSNGSAGSEHSINGRRFPVEaedacrgdimlmlsqgmrfillglkkeqfeerkswttyqsMQIF 217
Cdd:smart01057   78 PLPGRYRLKQFHFHWG-GSDSEGSEHTIDGKRFPLE----------------------------------------LHLV 116

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   218 FYNPDDfdSFQTAISENRIIGAMAIFFQVSPRDNSALDPIIHGLKGVVHHEKETFLDPFVLRDLLPASLGSYYRYTGSLT 297
Cdd:smart01057  117 HYNSKG--SFSEAVSKPGGLAVVAVFFKVGAEENPALQAILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLT 194

                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591655   298 TPPCSEIVEWIVFRRPVPISYHQLEAFYSIFTTEQQdhvksvEYLRNNFRPQQRLHDRV 356
Cdd:smart01057  195 TPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN------EPLVNNARPLQPLNGRV 247
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
67-360 6.45e-88

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 286.47  E-value: 6.45e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   67 GPEHWVTSSVSCGGRHQSPIDILDQYARVGEEYQELQLDGFDNESSNKTwMKNTGKTVAILLKDDY--FVSGAGLPGRFK 144
Cdd:pfam00194    2 GPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNT-LTNNGHTVQVSLDDGDpsTISGGPLATRYR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  145 AEKVEFHWGhSNGSAGSEHSINGRRFPVEaedacrgdimlmlsqgmrfillglkkeqfeerkswttyqsMQIFFYNpDDF 224
Cdd:pfam00194   81 LVQFHFHWG-STDSRGSEHTIDGKRYPAE----------------------------------------LHIVHYN-SKY 118

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  225 DSFQTAISENRIIGAMAIFFQVSPRDNSALDPIIHGLKGVVHHEKETFLDPFVLRDLLPASLGSYYRYTGSLTTPPCSEI 304
Cdd:pfam00194  119 KSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALDNIKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSES 198

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591655  305 VEWIVFRRPVPISYHQLEAFYSIFTTEQQDHvksVEYLRNNFRPQQRLHDRVVSKS 360
Cdd:pfam00194  199 VTWIVFKEPISISEEQLEAFRTLLFSDGGEE---PRPLVNNFRPTQPLNGRVVFAS 251
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1161-1419 2.39e-78

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 259.51  E-value: 2.39e-78
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  1161 LEKQFKLVTQCNAKYVECFSAQKECNKEKNRNSSVVPSERARVGLAPLPGmKGTDYINASYIMGYYRSNEFIITQHPLPH 1240
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  1241 TTKDFWRMIWDHNAQIIVMLPDNQSL-AEDEFVYWPSRE-ESMNCEAFTVTLISKDRLclsneEQIIIHDFILEATQDDY 1318
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKgREKCAQYWPDEEgEPLTYGDITVTLKSVEKV-----DDYTIRTLEVTNTGCSE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  1319 VLEVRHFQCPKWPNPDAP--ISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKM 1396
Cdd:smart00194  156 TRTVTHYHYTNWPDHGVPesPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKE 235

                           250       260
                    ....*....|....*....|...
gi 2462591655  1397 INLMRPGVFTDIEQYQFIYKAML 1419
Cdd:smart00194  236 LRSQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1186-1419 7.90e-78

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 257.17  E-value: 7.90e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1186 NKEKNRNSSVVPSERARVGLAPLPGmkGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQS 1265
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG--PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1266 LA-EDEFVYWP-SREESMNCEAFTVTLISKDrlclSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAP--ISSTF 1341
Cdd:pfam00102   79 KGrEKCAQYWPeEEGESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPesPNSLL 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591655 1342 ELINVIKEEALT-RDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAML 1419
Cdd:pfam00102  155 DLLRKVRKSSLDgRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PHA02738 PHA02738
hypothetical protein; Provisional
 862-1127 3.37e-46

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 169.34  E-value: 3.37e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  862 DFEEVqrctadmnITAEH------------SNHPENKHKNRYINILAYDHSRVKLRplpgKDSKHSDYINANYVDGYNKA 929
Cdd:PHA02738    22 DCEEV--------ITREHqkvisekvdgtfNAEKKNRKLNRYLDAVCFDHSRVILP----AERNRGDYINANYVDGFEYK 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  930 KAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPT--ENSEEYGNIIVTLKSTKIHACYtvrrfsI 1007
Cdd:PHA02738    90 KKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDveQGSIRFGKFKITTTQVETHPHY------V 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1008 RNTKVKKgqkgnpKGRQNERVVIQYHYTQWPDMGVPEYALPVLTFV------RRSSAARMPETG-------PVLVHCSAG 1074
Cdd:PHA02738   164 KSTLLLT------DGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVlevrqcQKELAQESLQIGhnrlqppPIVVHCNAG 237

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462591655 1075 VGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDAL 1127
Cdd:PHA02738   238 LGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
879-1123 6.09e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 158.72  E-value: 6.09e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  879 HSNHPENKHKNRYINILAYDHSRVklrplpGKDSKhsdYINANYVDGYNKaKAYIATQGPLKSTFEDFWRMIWEQNTGII 958
Cdd:COG5599     36 YLQNINGSPLNRFRDIQPYKETAL------RANLG---YLNANYIQVIGN-HRYIATQYPLEEQLEDFFQMLFDNNTPVL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  959 VMITNLVE--KGRRKCDQYWPTenSEEYGNIIVTLKSTKIHACYTvrRFSIRNTKVKKGQKGnpkgrQNERVVIQYHYTQ 1036
Cdd:COG5599    106 VVLASDDEisKPKVKMPVYFRQ--DGEYGKYEVSSELTESIQLRD--GIEARTYVLTIKGTG-----QKKIEIPVLHVKN 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1037 WPDMGVP--EYALPVLTFVRRSSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKS--TVNVLGFLKHIRTQRNY 1112
Cdd:COG5599    177 WPDHGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRNG 256

                          250
                   ....*....|..
gi 2462591655 1113 -LVQTEEQYIFI 1123
Cdd:COG5599    257 gMVQTSEQLDVL 268
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
53-360 3.32e-37

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 140.79  E-value: 3.32e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   53 KASGDPYWAYSGAYGPEHWVTSSVS---CG-GRHQSPIDILDQyarVGEEYQELQldgFDNESSNKTwMKNTGKTVAILL 128
Cdd:COG3338     21 AAASAPHWSYEGETGPEHWGELSPEfatCAtGKNQSPIDIRTA---IKADLPPLK---FDYKPTPLE-IVNNGHTIQVNV 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  129 KDDYFVSGAGLpgRFKAEKVEFHwghsngsAGSEHSINGRRFPVEAedacrgdimlmlsqgmrfillglkkeQFEERksw 208
Cdd:COG3338     94 DPGSTLTVDGK--RYELKQFHFH-------TPSEHTINGKSYPMEA--------------------------HLVHK--- 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  209 ttyqsmqiffyNPDDfdsfQTAIsenriigaMAIFFQVSpRDNSALDPIIHGL---KGvvhhEKETFLDPFVLRDLLPAS 285
Cdd:COG3338    136 -----------DADG----ELAV--------VGVLFEEG-AENPALAKLWANLpleAG----EEVALDATIDLNDLLPED 187

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462591655  286 LgSYYRYTGSLTTPPCSEIVEWIVFRRPVPISYHQLEAFYSIFtteqqdhvksveylRNNFRPQQRLHDRVVSKS 360
Cdd:COG3338    188 R-SYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAFARLY--------------PNNARPVQPLNGRLILES 247
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1157-1427 4.51e-24

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 104.70  E-value: 4.51e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1157 GKTRLEkQFKLVTQCNAKYVECFsaQKECNKEKNRNSSVVPSERARVGLAPLPGmKGTDYINASYIMGYYRSNEFIITQH 1236
Cdd:PHA02747    25 GIIRDE-HHQIILKPFDGLIANF--EKPENQPKNRYWDIPCWDHNRVILDSGGG-STSDYIHANWIDGFEDDKKFIATQG 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1237 PLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE--FVYW-PSREESMNCEAFTVTLISKDRLCLSNEEQIIIHDFILEA 1313
Cdd:PHA02747   101 PFAETCADFWKAVWQEHCSIIVMLTPTKGTNGEEkcYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKD 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1314 TQddyvlEVRHFQCPKWPNPDAPISST-----FELINVIKEEALTRDG-------PTIVHDEYGAVSAGMLCALTTLSQQ 1381
Cdd:PHA02747   181 SR-----KISHFQCSEWFEDETPSDHPdfikfIKIIDINRKKSGKLFNpkdallcPIVVHCSDGVGKTGIFCAVDICLNQ 255

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2462591655 1382 LENENAVDVFQVAKMINLMRPGVFTDIEQYQFI---YKAMLSLVSTKEN 1427
Cdd:PHA02747   256 LVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIqpgYEVLHYFLSKIKA 304
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 388-478 3.83e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 55.20  E-value: 3.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  388 SPPIHMKVQPLNQTALQVSWSQPETIyHPPIMNYMISYSWTKNEDEKEktFTKDSDKDLKATISHVSPDSLYLFRVQAVc 467
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEDD-GGPITGYVVEYREKGSGDWKE--VEVTPGSETSYTLTGLKPGTEYEFRVRAV- 77

                           90
                   ....*....|.
gi 2462591655  468 RNDMRSDFSQT 478
Cdd:cd00063     78 NGGGESPPSES 88
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 388-466 5.67e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 54.54  E-value: 5.67e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591655   388 SPPIHMKVQPLNQTALQVSWSQPEtiyHPPIMNYMISYSWTKNEDEKEKTFTKDSDKDLKATISHVSPDSLYLFRVQAV 466
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
PLN02179 PLN02179
carbonic anhydrase
 17-312 2.62e-08

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 56.14  E-value: 2.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   17 TSSVLHYVVCFPALTEGYVGALHENRHGSA--VQIRRRKASGDPYWaysGAYGPeHWvtsSVSCGGRHQSPIDILDQyaR 94
Cdd:PLN02179     5 TKTIFFFVVFFIDLFFPNILLVYAREIGNKplFTYKQKTEKGPAEW---GKLNP-QW---KVCSTGKYQSPIDLTDE--R 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   95 VGEEYqelqldgfdnessNKTWMKNTGKTVAILLK--DDYFVSGAGLPGRFKAEKVEF-----HWgHSNgsagSEHSING 167
Cdd:PLN02179    76 VSLIH-------------DQALSRHYKPAPAVIQSrgHDVMVSWKGDAGKITIHQTDYklvqcHW-HSP----SEHTING 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  168 RRFPVEAEdacrgdiMLMLSQGMRFILLGLKKEQFEerkswttyqsmqiffynPDDFdsfqtaisenriigamaiffqvs 247
Cdd:PLN02179   138 TSYDLELH-------MVHTSASGKTAVVGVLYKLGE-----------------PDEF----------------------- 170

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591655  248 prdnsaLDPIIHGLKGVVHHEKET-FLDPFVLRdllpASLGSYYRYTGSLTTPPCSEIVEWIVFRR 312
Cdd:PLN02179   171 ------LTKLLNGIKGVGKKEINLgIVDPRDIR----FETNNFYRYIGSLTIPPCTEGVIWTVVKR 226
fn3 pfam00041
Fibronectin type III domain;
388-466 3.65e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 52.03  E-value: 3.65e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591655  388 SPPIHMKVQPLNQTALQVSWSQPETiYHPPIMNYMISYsWTKNEDEKEKTFTKDSDKDlKATISHVSPDSLYLFRVQAV 466
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPD-GNGPITGYEVEY-RPKNSGEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAV 76
PHA03169 PHA03169
hypothetical protein; Provisional
 584-742 7.88e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 49.97  E-value: 7.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  584 ASKQAARPVLATTealASPGPDGDSSPtkDGEGTEEGEKDEKSESEDGEREHEEDGEKDSEKKEKSGVTHAAEERNQtEP 663
Cdd:PHA03169   105 PSPSGSAEELASG---LSPENTSGSSP--ESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPE-EP 178

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591655  664 SPTPSSPNRTAEGGHQTIPGHEQDHTAVPTDQTGgrRDAGPGldPDMVTSTQVPPTATEEQYAgSDPKRPEMPSKKPMS 742
Cdd:PHA03169   179 EPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPG--EPQSPT--PQQAPSPNTQQAVEHEDEP-TEPEREGPPFPGHRS 252
 
Name Accession Description Interval E-value
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 859-1132 0e+00

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG has four splicing isoforms: three transmembrane isoforms, PTPRG-A, B, and C, and one secretory isoform, PTPRG-S, which are expressed in many tissues including the brain. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 635.92  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  859 FSEDFEEVQRCTADMNITAEHSNHPENKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 938
Cdd:cd17667      1 FSEDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  939 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKG 1018
Cdd:cd17667     81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1019 NPKGRQNERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 1098
Cdd:cd17667    161 NPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 240

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2462591655 1099 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 1132
Cdd:cd17667    241 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1216-1420 8.87e-158

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 474.17  E-value: 8.87e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFVYWPSREESMNCEAFTVTLISKDR 1295
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNCEAFTVTLISKDR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1296 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGMLCAL 1375
Cdd:cd17670     81 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEFGAVSAGTLCAL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2462591655 1376 TTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAMLS 1420
Cdd:cd17670    161 TTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 917-1125 1.72e-149

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 452.19  E-value: 1.72e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKI 996
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  997 HACYTVRRFSIRNTKVKKgqkgnPKGRQNERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPETGPVLVHCSAGVG 1076
Cdd:cd14549     81 LATYTVRTFSLKNLKLKK-----VKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVG 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2462591655 1077 RTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHD 1125
Cdd:cd14549    156 RTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1216-1419 1.04e-136

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 418.24  E-value: 1.04e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFVYWPSREESMNCEAFTVTLISKDR 1295
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEEH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1296 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGMLCAL 1375
Cdd:cd17669     81 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2462591655 1376 TTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAML 1419
Cdd:cd17669    161 TTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 917-1128 2.56e-134

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 412.06  E-value: 2.56e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKI 996
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  997 HACYTVRRFSIRNTKVKKGQKgnpKGRQNERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPETGPVLVHCSAGVG 1076
Cdd:cd17668     81 LAYYTVRNFTLRNTKIKKGSQ---KGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVG 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462591655 1077 RTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALL 1128
Cdd:cd17668    158 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1216-1416 1.29e-124

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 385.52  E-value: 1.29e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQsLAEDEFVYWPSREESMNCEAFTVTLISKDR 1295
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNE-LNEDEPIYWPTKEKPLECETFKVTLSGEDH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1296 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGMLCAL 1375
Cdd:cd14550     80 SCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAATFCAL 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2462591655 1376 TTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYK 1416
Cdd:cd14550    160 TTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
858-1129 2.13e-119

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 373.92  E-value: 2.13e-119
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   858 GFSEDFEEVQRCTADMnITAEHSNHPENKHKNRYINILAYDHSRVKLRPLPGKDSkhsDYINANYVDGYNKAKAYIATQG 937
Cdd:smart00194    1 GLEEEFEKLDRLKPDD-ESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGS---DYINASYIDGPNGPKAYIATQG 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   938 PLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE--EYGNIIVTLKSTKIHACYTVRRFSIRNTkvkkg 1015
Cdd:smart00194   77 PLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNT----- 151

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  1016 qkgnpkGRQNERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKS 1095
Cdd:smart00194  152 ------GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK 225

                           250       260       270
                    ....*....|....*....|....*....|....
gi 2462591655  1096 TVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1129
Cdd:smart00194  226 EVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 885-1131 9.03e-116

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 363.25  E-value: 9.03e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  885 NKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNL 964
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGVPG--SDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  965 VEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTkvkkgqkgnpkGRQNERVVIQYHYTQWPDMGVPE 1044
Cdd:cd14553     81 EERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKN-----------GSSEKREVRQFQFTAWPDHGVPE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1045 YALPVLTFVRRSSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1124
Cdd:cd14553    150 HPTPFLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIH 229


                   ....*..
gi 2462591655 1125 DALLEAI 1131
Cdd:cd14553    230 DALLEAV 236
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 67-359 3.70e-115

Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related proteins (CARPs) are sequence similar to carbonic anhydrases. Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism. CARPs have lost conserved histidines involved in zinc binding and consequently their catalytic activity. This sub-family of carbonic anhydrase-related domains found in tyrosine phosphatase receptors may play a role in cell adhesion.


Pssm-ID: 239396 [Multi-domain]  Cd Length: 253  Bit Score: 362.06  E-value: 3.70e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   67 GPEHWVTSSVSCG-GRHQSPIDILDQYARVGEEYQELQLDGFDNESsNKTWMKNTGKTVAILLKD---DYFVSGAGLPGR 142
Cdd:cd03122      1 NPKHWAKKYPACGeGRQQSPIDIVEDTQVQRQGLQPLHFDGYEELT-ASTTLENTGKTVILRLEGnssDPFVSGGPLLGR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  143 FKAEKVEFHWGHSNgSAGSEHSINGRRFPVEaedacrgdimlmlsqgmrfillglkkeqfeerkswttyqsMQIFFYNPD 222
Cdd:cd03122     80 YKFSEITFHWGTCN-SDGSEHSIDGHKFPLE----------------------------------------MQILHRNTD 118

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  223 DFDSFqTAISENRIIGAMAIFFQVSPRDNSALDPIIHGLKGVVHHEKETFLDPFVLRDLLPASLGSYYRYTGSLTTPPCS 302
Cdd:cd03122    119 FFDSF-EAIKSPGGVLALAYLFELSHEDNPFLDPIIEGLRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCS 197

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462591655  303 EIVEWIVFRRPVPISYHQLEAFYSIFTTEQQDhVKSVEYLRNNFRPQQRLHDRVVSK 359
Cdd:cd03122    198 ETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGDYLPNNGRPQQPLGSRTVFS 253
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
885-1129 6.99e-112

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 352.31  E-value: 6.99e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  885 NKHKNRYINILAYDHSRVKLRPLPGkdskHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNL 964
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG----PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  965 VEKGRRKCDQYWPTEN--SEEYGNIIVTLKSTKIH-ACYTVRRFSIRNTKVKKgqkgnpkgrqnERVVIQYHYTQWPDMG 1041
Cdd:pfam00102   77 EEKGREKCAQYWPEEEgeSLEYGDFTVTLKKEKEDeKDYTVRTLEVSNGGSEE-----------TRTVKHFHYTGWPDHG 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1042 VPEYALPVLTFVRR-SSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQY 1120
Cdd:pfam00102  146 VPESPNSLLDLLRKvRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQY 225


                   ....*....
gi 2462591655 1121 IFIHDALLE 1129
Cdd:pfam00102  226 IFLYDAILE 234
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 847-1131 2.65e-99

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 319.29  E-value: 2.65e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  847 HIGELYSNNQHGFSEDFEEVQrctADMNITAEHSNHPENKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGY 926
Cdd:cd14626      6 NIERLKANDGLKFSQEYESID---PGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPG--SDYINANYIDGY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  927 NKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFS 1006
Cdd:cd14626     81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1007 IRNTkvkkgqkgnpkGRQNERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPETGPVLVHCSAGVGRTGTYIVIDS 1086
Cdd:cd14626    161 LYKN-----------GSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDA 229

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2462591655 1087 MLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 1131
Cdd:cd14626    230 MLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 917-1125 3.20e-96

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 307.67  E-value: 3.20e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE--EYGNIIVTLKST 994
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKplEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  995 KIHACYTVRRFSIRNTKVKkgqkgnpkgrqNERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPETGPVLVHCSAG 1074
Cdd:cd00047     81 EELSDYTIRTLELSPKGCS-----------ESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAG 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462591655 1075 VGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHD 1125
Cdd:cd00047    150 VGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 839-1131 8.71e-96

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 309.72  E-value: 8.71e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  839 IPVKQFVKHIGELYSNNQHGFSEDFEEVQrctADMNITAEHSNHPENKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYI 918
Cdd:cd14625      4 IPISELAEHTERLKANDNLKLSQEYESID---PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMG--SDYI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  919 NANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHA 998
Cdd:cd14625     79 NANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLDTIELA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  999 CYTVRRFSIRNTkvkkgqkgnpkGRQNERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPETGPVLVHCSAGVGRT 1078
Cdd:cd14625    159 TFCVRTFSLHKN-----------GSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRT 227

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462591655 1079 GTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 1131
Cdd:cd14625    228 GCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 839-1131 2.00e-93

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 303.19  E-value: 2.00e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  839 IPVKQFVKHIGELYSNNQHGFSEDFEEVQrctADMNITAEHSNHPENKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYI 918
Cdd:cd14624      4 IPILELADHIERLKANDNLKFSQEYESID---PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPG--SDYI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  919 NANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHA 998
Cdd:cd14624     79 NANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGLIQVTLLDTVELA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  999 CYTVRRFSIRNTkvkkgqkgnpkGRQNERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPETGPVLVHCSAGVGRT 1078
Cdd:cd14624    159 TYCVRTFALYKN-----------GSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRT 227

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462591655 1079 GTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 1131
Cdd:cd14624    228 GCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 890-1124 4.55e-92

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 296.96  E-value: 4.55e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  890 RYINILAYDHSRVKLRPLPgkDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGR 969
Cdd:cd14548      1 RYTNILPYDHSRVKLIPIN--EEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  970 RKCDQYWPTENSE-EYGNIIVTLKSTKIHACYTVRRFSIrntkvkkgqkgnpKGRQNERVVIQYHYTQWPDMGVPEYALP 1048
Cdd:cd14548     79 VKCDHYWPFDQDPvYYGDITVTMLSESVLPDWTIREFKL-------------ERGDEVRSVRQFHFTAWPDHGVPEAPDS 145

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591655 1049 VLTFVRRSSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1124
Cdd:cd14548    146 LLRFVRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
 60-356 3.86e-90

Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse the reversible hydration of carbon dioxide to bicarbonate.. CAs have essential roles in facilitating the transport of carbon dioxide and protons in the intracellular space, across biological membranes and in the layers of the extracellular space; they are also involved in many other processes, from respiration and photosynthesis in eukaryotes to cyanate degradation in prokaryotes. There are five known evolutionarily distinct CA families (alpha, beta, gamma, delta and epsilon) that have no significant sequence identity and have structurally distinct overall folds. Some CAs are membrane-bound, while others act in the cytosol; there are several related proteins that lack enzymatic activity. The active site of alpha-CAs is well described, consisting of a zinc ion coordinated through 3 histidine residues and a water molecule/hydroxide ion that acts as a potent nucleophile. The enzyme employs a two-step mechanism: in the first step, there is a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide; in the second step, the active site is regenerated by the ionisation of the zinc-bound water molecule and the removal of a proton from the active site. Beta- and gamma-CAs also employ a zinc hydroxide mechanism, although at least some beta-class enzymes do not have water directly coordinated to the metal ion.


Pssm-ID: 215000 [Multi-domain]  Cd Length: 247  Bit Score: 292.30  E-value: 3.86e-90
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655    60 WAYSGAYGPEHWVTSS-VSCGGRHQSPIDILDQYARVGEEYQELQldgFDNESSNKTWMKNTGKTVAILLKDD-YFVSGA 137
Cdd:smart01057    1 WGYEGKNGPEHWGKLDpPFCGGKRQSPIDIVTAEAQYDPSLKPLK---LSYDQPTAKRILNNGHTVQVNFDDDgSTLSGG 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   138 GLPGRFKAEKVEFHWGhSNGSAGSEHSINGRRFPVEaedacrgdimlmlsqgmrfillglkkeqfeerkswttyqsMQIF 217
Cdd:smart01057   78 PLPGRYRLKQFHFHWG-GSDSEGSEHTIDGKRFPLE----------------------------------------LHLV 116

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   218 FYNPDDfdSFQTAISENRIIGAMAIFFQVSPRDNSALDPIIHGLKGVVHHEKETFLDPFVLRDLLPASLGSYYRYTGSLT 297
Cdd:smart01057  117 HYNSKG--SFSEAVSKPGGLAVVAVFFKVGAEENPALQAILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLT 194

                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591655   298 TPPCSEIVEWIVFRRPVPISYHQLEAFYSIFTTEQQdhvksvEYLRNNFRPQQRLHDRV 356
Cdd:smart01057  195 TPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN------EPLVNNARPLQPLNGRV 247
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 856-1124 2.29e-89

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 291.19  E-value: 2.29e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  856 QHGFSEDFEEVQRCTADMniTAEHSNHPENKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIAT 935
Cdd:cd14543      2 KRGIYEEYEDIRREPPAG--TFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDER--TDYINANFMDGYKQKNAYIAT 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  936 QGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTE--NSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVK 1013
Cdd:cd14543     78 QGPLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEegSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETD 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1014 KGqkgnpkgrqneRVVIQYHYTQWPDMGVPEYALPVLTF---VRRSSAARMPETG----------PVLVHCSAGVGRTGT 1080
Cdd:cd14543    158 ES-----------RQVTHFQFTSWPDFGVPSSAAALLDFlgeVRQQQALAVKAMGdrwkghppgpPIVVHCSAGIGRTGT 226

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2462591655 1081 YIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1124
Cdd:cd14543    227 FCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
67-360 6.45e-88

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 286.47  E-value: 6.45e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   67 GPEHWVTSSVSCGGRHQSPIDILDQYARVGEEYQELQLDGFDNESSNKTwMKNTGKTVAILLKDDY--FVSGAGLPGRFK 144
Cdd:pfam00194    2 GPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNT-LTNNGHTVQVSLDDGDpsTISGGPLATRYR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  145 AEKVEFHWGhSNGSAGSEHSINGRRFPVEaedacrgdimlmlsqgmrfillglkkeqfeerkswttyqsMQIFFYNpDDF 224
Cdd:pfam00194   81 LVQFHFHWG-STDSRGSEHTIDGKRYPAE----------------------------------------LHIVHYN-SKY 118

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  225 DSFQTAISENRIIGAMAIFFQVSPRDNSALDPIIHGLKGVVHHEKETFLDPFVLRDLLPASLGSYYRYTGSLTTPPCSEI 304
Cdd:pfam00194  119 KSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALDNIKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSES 198

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591655  305 VEWIVFRRPVPISYHQLEAFYSIFTTEQQDHvksVEYLRNNFRPQQRLHDRVVSKS 360
Cdd:pfam00194  199 VTWIVFKEPISISEEQLEAFRTLLFSDGGEE---PRPLVNNFRPTQPLNGRVVFAS 251
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 884-1132 1.36e-84

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 276.52  E-value: 1.36e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  884 ENKHKNRYINILAYDHSRVKLRPLPGkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITN 963
Cdd:cd14630      2 ENRNKNRYGNIISYDHSRVRLQLLDG--DPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  964 LVEKGRRKCDQYWPtENSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgnpKGRQNERVVIQYHYTQWPDMGVP 1043
Cdd:cd14630     80 LVEVGRVKCVRYWP-DDTEVYGDIKVTLIETEPLAEYVIRTFTVQK-----------KGYHEIREIRQFHFTSWPDHGVP 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1044 EYALPVLTFVRRSSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFI 1123
Cdd:cd14630    148 CYATGLLGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFV 227


                   ....*....
gi 2462591655 1124 HDALLEAIL 1132
Cdd:cd14630    228 HDAILEACL 236
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 839-1138 8.27e-84

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350469 [Multi-domain]  Cd Length: 296  Bit Score: 276.52  E-value: 8.27e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  839 IPVKQFVKHIGELYSNNQHGFSEDFEEVQRCTadMNITAEHSNHPENKHKNRYINILAYDHSRVKLRPLPGkdSKHSDYI 918
Cdd:cd14621      8 LPVDKLEEEINRRMADDNKLFREEFNALPACP--IQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEG--VPDSDYI 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  919 NANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHA 998
Cdd:cd14621     84 NASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVTVLV 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  999 CYTVRRFSIRntkvkkgQKGNPKGRQNERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPETGPVLVHCSAGVGRT 1078
Cdd:cd14621    164 DYTVRKFCIQ-------QVGDVTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRT 236

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1079 GTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAILGKETEV 1138
Cdd:cd14621    237 GTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 844-1132 1.45e-79

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 263.44  E-value: 1.45e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  844 FVKHIGELYSNNQHGFSEDFE---EVQRCTADmnitaeHSNHPENKHKNRYINILAYDHSRVKLRPLPGKdsKHSDYINA 920
Cdd:cd14633      2 LLQHITQMKCAEGYGFKEEYEsffEGQSAPWD------SAKKDENRMKNRYGNIIAYDHSRVRLQPIEGE--TSSDYING 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  921 NYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPtENSEEYGNIIVTLKSTKIHACY 1000
Cdd:cd14633     74 NYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP-DDTEIYKDIKVTLIETELLAEY 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1001 TVRRFSIRNtkvkkgqkgnpKGRQNERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPETGPVLVHCSAGVGRTGT 1080
Cdd:cd14633    153 VIRTFAVEK-----------RGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGC 221

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462591655 1081 YIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 1132
Cdd:cd14633    222 FIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 889-1124 2.13e-78

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 258.31  E-value: 2.13e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  889 NRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKG 968
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNV--DDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  969 RRKCDQYWPTE-NSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkvkKGQKGNPkgrqneRVVIQYHYTQWPDMGVPEYAL 1047
Cdd:cd14617     79 RVKCDHYWPADqDSLYYGDLIVQMLSESVLPEWTIREFKICS----EEQLDAP------RLVRHFHYTVWPDHGVPETTQ 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591655 1048 PVLTFVR--RSSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1124
Cdd:cd14617    149 SLIQFVRtvRDYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1161-1419 2.39e-78

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 259.51  E-value: 2.39e-78
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  1161 LEKQFKLVTQCNAKYVECFSAQKECNKEKNRNSSVVPSERARVGLAPLPGmKGTDYINASYIMGYYRSNEFIITQHPLPH 1240
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  1241 TTKDFWRMIWDHNAQIIVMLPDNQSL-AEDEFVYWPSRE-ESMNCEAFTVTLISKDRLclsneEQIIIHDFILEATQDDY 1318
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKgREKCAQYWPDEEgEPLTYGDITVTLKSVEKV-----DDYTIRTLEVTNTGCSE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  1319 VLEVRHFQCPKWPNPDAP--ISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKM 1396
Cdd:smart00194  156 TRTVTHYHYTNWPDHGVPesPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKE 235

                           250       260
                    ....*....|....*....|...
gi 2462591655  1397 INLMRPGVFTDIEQYQFIYKAML 1419
Cdd:smart00194  236 LRSQRPGMVQTEEQYIFLYRAIL 258
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1186-1419 7.90e-78

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 257.17  E-value: 7.90e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1186 NKEKNRNSSVVPSERARVGLAPLPGmkGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQS 1265
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG--PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1266 LA-EDEFVYWP-SREESMNCEAFTVTLISKDrlclSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAP--ISSTF 1341
Cdd:pfam00102   79 KGrEKCAQYWPeEEGESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPesPNSLL 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591655 1342 ELINVIKEEALT-RDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAML 1419
Cdd:pfam00102  155 DLLRKVRKSSLDgRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 889-1129 2.87e-77

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 255.13  E-value: 2.87e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  889 NRYINILAYDHSRVKLRPLpgkDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKG 968
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQ---SHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  969 RRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkVKKGQKgnpkgrqneRVVIQYHYTQWPDMGVPEYALP 1048
Cdd:cd14615     78 RTKCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKN--AQTNES---------RTVRHFHFTSWPDHGVPETTDL 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1049 VLTF--VRRSSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDA 1126
Cdd:cd14615    147 LINFrhLVREYMKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQC 226


                   ...
gi 2462591655 1127 LLE 1129
Cdd:cd14615    227 ALD 229
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
 80-357 4.58e-76

Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues and a fourth conserved histidine plays a potential role in proton transfer.


Pssm-ID: 238200  Cd Length: 227  Bit Score: 251.82  E-value: 4.58e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   80 GRHQSPIDILDQYARVGEEYQELQLDGFDNESsnkTWMKNTGKTVAILLKDD-YFVSGAGLPGRFKAEKVEFHWGhSNGS 158
Cdd:cd00326      1 GKRQSPINIVTSAVVYDPSLPPLNFDYYPTTS---LTLVNNGHTVQVNFDDDgGTLSGGGLPGRYKLVQFHFHWG-SENS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  159 AGSEHSINGRRFPVEaedacrgdimlmlsqgmrfillglkkeqfeerkswttyqsMQIFFYNPDDFDSfqTAISENRIIG 238
Cdd:cd00326     77 PGSEHTIDGKRYPLE----------------------------------------LHLVHYNSDYYSS--EAAKKPGGLA 114

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  239 AMAIFFQVSPRDNSALDPIIHGLKGVVHHEKETFLDPFVLRDLLPASLGSYYRYTGSLTTPPCSEIVEWIVFRRPVPISY 318
Cdd:cd00326    115 VLGVFFEVGEKENPFLKKILDALPKIKYKGKETTLPPFDLSDLLPSSLRDYYTYEGSLTTPPCSEGVTWIVFKEPITISK 194

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2462591655  319 HQLEAFYSIFTTEqqdhvksVEYLRNNFRPQQRLHDRVV 357
Cdd:cd00326    195 EQLEAFRSLLDRE-------GKPLVNNYRPVQPLNGRVV 226
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 889-1124 9.81e-76

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 250.78  E-value: 9.81e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  889 NRYINILAYDHSRVKLRPLPgkDSKHSDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEK 967
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVD--DDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  968 gRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgnpkgRQNERVVIQYHYTQWPDMGVPEYAL 1047
Cdd:cd14547     79 -KEKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKY-------------GGEKRYLKHYWYTSWPDHKTPEAAQ 144

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591655 1048 PVLTFVRR--SSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1124
Cdd:cd14547    145 PLLSLVQEveEARQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 917-1132 1.22e-75

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 249.45  E-value: 1.22e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPtENSEEYGNIIVTLKSTKI 996
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP-DDTEVYGDIKVTLVETEP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  997 HACYTVRRFSIRNtkvkkgqkgnpKGRQNERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPETGPVLVHCSAGVG 1076
Cdd:cd14555     80 LAEYVVRTFALER-----------RGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAG 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591655 1077 RTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 1132
Cdd:cd14555    149 RTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 891-1129 1.47e-74

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).


Pssm-ID: 350468 [Multi-domain]  Cd Length: 229  Bit Score: 247.55  E-value: 1.47e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  891 YINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRR 970
Cdd:cd14620      1 YPNILPYDHSRVILSQLDGIPC--SDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  971 KCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIrntkvkkgQKGNPKGRQNERVVIQYHYTQWPDMGVPEYALPVL 1050
Cdd:cd14620     79 KCYQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCI--------QPQLPDGCKAPRLVTQLHFTSWPDFGVPFTPIGML 150

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591655 1051 TFVRRSSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1129
Cdd:cd14620    151 KFLKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 880-1128 3.12e-74

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 247.05  E-value: 3.12e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  880 SNHPENKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIV 959
Cdd:cd14554      1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEG--SDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  960 MITNLVEKGRRKCDQYWPTENSEEYGNIIVtlkstKIHACYTVRRFSIRNTKVKKGQKGnpkgrqNERVVIQYHYTQWPD 1039
Cdd:cd14554     79 MLTKLREMGREKCHQYWPAERSARYQYFVV-----DPMAEYNMPQYILREFKVTDARDG------QSRTVRQFQFTDWPE 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1040 MGVPEYALPVLTFVRR--SSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTE 1117
Cdd:cd14554    148 QGVPKSGEGFIDFIGQvhKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTE 227

                          250
                   ....*....|.
gi 2462591655 1118 EQYIFIHDALL 1128
Cdd:cd14554    228 DQYQFCYRAAL 238
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 889-1131 2.04e-73

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 244.41  E-value: 2.04e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  889 NRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKG 968
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPI--HEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  969 RRKCDQYWPTENSE-EYGNIIVTLKSTKIHACYTVRRFSIRNTKvkkgqkgnpkgRQNERVVIQYHYTQWPDMGVPEYAL 1047
Cdd:cd14619     79 RVKCEHYWPLDYTPcTYGHLRVTVVSEEVMENWTVREFLLKQVE-----------EQKTLSVRHFHFTAWPDHGVPSSTD 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1048 PVLTFVR--RSSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHD 1125
Cdd:cd14619    148 TLLAFRRllRQWLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQ 227


                   ....*.
gi 2462591655 1126 ALLEAI 1131
Cdd:cd14619    228 CILDFL 233
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 885-1127 1.60e-72

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 242.75  E-value: 1.60e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  885 NKHKNRYINILAYDHSRVKLRPLPgKDSKHSDYINANYVDGYN-------KAKAYIATQGPLKSTFEDFWRMIWEQNTGI 957
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRD-PNVPGSDYINANYIRNENegpttdeNAKTYIATQGCLENTVSDFWSMVWQENSRV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  958 IVMITNLVEKGRRKCDQYWPTE-NSEEYGNIIVTLKSTKIHACYTVRRFsirntKVKKGQKGNPkgrqnERVVIQYHYTQ 1036
Cdd:cd14544     80 IVMTTKEVERGKNKCVRYWPDEgMQKQYGPYRVQNVSEHDTTDYTLREL-----QVSKLDQGDP-----IREIWHYQYLS 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1037 WPDMGVPEYALPVLTFV----RRSSAarMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKS---TVNVLGFLKHIRTQ 1109
Cdd:cd14544    150 WPDHGVPSDPGGVLNFLedvnQRQES--LPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQ 227

                          250
                   ....*....|....*...
gi 2462591655 1110 RNYLVQTEEQYIFIHDAL 1127
Cdd:cd14544    228 RSGMVQTEAQYKFIYVAV 245
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 874-1124 1.18e-71

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 239.79  E-value: 1.18e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  874 NITAEHSNHPENKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQ 953
Cdd:cd14614      1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSM--HEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  954 NTGIIVMITNLVEKGRRKCDQYWP-TENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTkvkkgqkgnpkgrQNERVVIQY 1032
Cdd:cd14614     79 KSQIIVMLTQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYA-------------DEVQDVMHF 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1033 HYTQWPDMGVP--EYALPVLTFVRRSSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQR 1110
Cdd:cd14614    146 NYTAWPDHGVPtaNAAESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYR 225

                          250
                   ....*....|....
gi 2462591655 1111 NYLVQTEEQYIFIH 1124
Cdd:cd14614    226 MSMVQTEEQYIFIH 239
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 889-1128 4.79e-71

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 237.53  E-value: 4.79e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  889 NRYINILAYDHSRVKLRPLPGKdsKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKG 968
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGE--PHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  969 RRKCDQYWPTENSE-EYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgnpKGRQNERVVIQYHYTQWPDMGVPEYAL 1047
Cdd:cd14618     79 RVLCDHYWPSESTPvSYGHITVHLLAQSSEDEWTRREFKLWH-----------EDLRKERRVKHLHYTAWPDHGIPESTS 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1048 PVLTFVR--RSSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHD 1125
Cdd:cd14618    148 SLMAFRElvREHVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHS 227


                   ...
gi 2462591655 1126 ALL 1128
Cdd:cd14618    228 CIL 230
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 917-1132 7.12e-71

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 236.10  E-value: 7.12e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPtENSEEYGNIIVTLKSTKI 996
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-DDSDTYGDIKITLLKTET 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  997 HACYTVRRFSIRNtkvkkgqkgnpKGRQNERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPETGPVLVHCSAGVG 1076
Cdd:cd14632     80 LAEYSVRTFALER-----------RGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAG 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591655 1077 RTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 1132
Cdd:cd14632    149 RTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACL 204
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 901-1132 8.37e-71

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 236.46  E-value: 8.37e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  901 RVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPtEN 980
Cdd:cd14631      1 RVILQPV--EDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  981 SEEYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgnpKGRQNERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAAR 1060
Cdd:cd14631     78 TEVYGDFKVTCVEMEPLAEYVVRTFTLER-----------RGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSN 146

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462591655 1061 MPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 1132
Cdd:cd14631    147 PPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 917-1125 2.91e-70

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 234.45  E-value: 2.91e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYVD-GYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE-EYGNIIVTLKST 994
Cdd:cd18533      1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEgEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  995 K--IHACYTVRRFSIRNTKVKKgqkgnpkgrqneRVVIQYHYTQWPDMGVPEYALPVLTFVRRSSA--ARMPETGPVLVH 1070
Cdd:cd18533     81 EenDDGGFIVREFELSKEDGKV------------KKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRElnDSASLDPPIIVH 148

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462591655 1071 CSAGVGRTGTYIVIDSMLQQIKDKSTVN---------VLGFLKHIRTQRNYLVQTEEQYIFIHD 1125
Cdd:cd18533    149 CSAGVGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 917-1124 6.26e-70

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 233.27  E-value: 6.26e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKI 996
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  997 HACYTVRRFSIRntkvkkgQKGNPKGRQNERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPETGPVLVHCSAGVG 1076
Cdd:cd14551     81 LVDYTTRKFCIQ-------KVNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVG 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2462591655 1077 RTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1124
Cdd:cd14551    154 RTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 880-1129 3.16e-65

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type tyrosine-protein phosphatase-like D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 223.45  E-value: 3.16e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  880 SNHPENKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIV 959
Cdd:cd14628     47 ANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVV 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  960 MITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIrnTKVKKGQkgnpkgrqnERVVIQYHYTQWPD 1039
Cdd:cd14628    125 MLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKV--TDARDGQ---------SRTVRQFQFTDWPE 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1040 MGVPEYALPVLTFVRR--SSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTE 1117
Cdd:cd14628    194 QGVPKSGEGFIDFIGQvhKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTE 273

                          250
                   ....*....|..
gi 2462591655 1118 EQYIFIHDALLE 1129
Cdd:cd14628    274 DQYQFCYRAALE 285
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 880-1129 5.10e-65

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 222.69  E-value: 5.10e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  880 SNHPENKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIV 959
Cdd:cd14627     48 ANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVV 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  960 MITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIrnTKVKKGQkgnpkgrqnERVVIQYHYTQWPD 1039
Cdd:cd14627    126 MLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKV--TDARDGQ---------SRTVRQFQFTDWPE 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1040 MGVPEYALPVLTFVRR--SSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTE 1117
Cdd:cd14627    195 QGVPKSGEGFIDFIGQvhKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTE 274

                          250
                   ....*....|..
gi 2462591655 1118 EQYIFIHDALLE 1129
Cdd:cd14627    275 DEYQFCYQAALE 286
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 917-1124 1.12e-64

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 218.16  E-value: 1.12e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPT--ENSEEYGNIIVTLKST 994
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmeEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  995 KIHACYTVRRFSIRNTKVKKGqkgnpkgrqnERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPETGPVLVHCSAG 1074
Cdd:cd14557     81 KICPDYIIRKLNINNKKEKGS----------GREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAG 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1075 VGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1124
Cdd:cd14557    151 VGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 880-1129 2.10e-63

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 218.06  E-value: 2.10e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  880 SNHPENKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIV 959
Cdd:cd14629     48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVV 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  960 MITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIrnTKVKKGQkgnpkgrqnERVVIQYHYTQWPD 1039
Cdd:cd14629    126 MLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKV--TDARDGQ---------SRTIRQFQFTDWPE 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1040 MGVPEYALPVLTFVRR--SSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTE 1117
Cdd:cd14629    195 QGVPKTGEGFIDFIGQvhKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTE 274

                          250
                   ....*....|..
gi 2462591655 1118 EQYIFIHDALLE 1129
Cdd:cd14629    275 DQYQLCYRAALE 286
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 886-1122 2.91e-63

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 215.33  E-value: 2.91e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  886 KHKNRYINILAYDHSRVKLRplpgkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLV 965
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKLK------QGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLM 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  966 EKGRRKCDQYWPTENSE----EYGNIIVTLKSTKIHACYTVRRFSIRNTKVkkgqkgnpkgrQNERVVIQYHYTQWPDMG 1041
Cdd:cd14545     75 EKGQIKCAQYWPQGEGNamifEDTGLKVTLLSEEDKSYYTVRTLELENLKT-----------QETREVLHFHYTTWPDFG 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1042 VPEYALPVLTFVR--RSSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDK--STVNVLGFLKHIRTQRNYLVQTE 1117
Cdd:cd14545    144 VPESPAAFLNFLQkvRESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGnpSSVDVKKVLLEMRKYRMGLIQTP 223


                   ....*
gi 2462591655 1118 EQYIF 1122
Cdd:cd14545    224 DQLRF 228
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 884-1131 8.82e-63

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 214.88  E-value: 8.82e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  884 ENKHKNRYINILAYDHSRVKLRPlPGKDSKHSDYINANYVDGYNKA--------KAYIATQGPLKSTFEDFWRMIWEQNT 955
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVLHD-GDPNEPVSDYINANIIMPEFETkcnnskpkKSYIATQGCLQNTVNDFWRMVFQENS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  956 GIIVMITNLVEKGRRKCDQYWPTENS-EEYGNIIV-TLKSTKIHacytvrRFSIRNTKVKKGQKGNpkgrqNERVVIQYH 1033
Cdd:cd14605     80 RVIVMTTKEVERGKSKCVKYWPDEYAlKEYGVMRVrNVKESAAH------DYILRELKLSKVGQGN-----TERTVWQYH 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1034 YTQWPDMGVPEYALPVLTFVRRSSAAR--MPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKST---VNVLGFLKHIRT 1108
Cdd:cd14605    149 FRTWPDHGVPSDPGGVLDFLEEVHHKQesIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRS 228

                          250       260
                   ....*....|....*....|...
gi 2462591655 1109 QRNYLVQTEEQYIFIHDALLEAI 1131
Cdd:cd14605    229 QRSGMVQTEAQYRFIYMAVQHYI 251
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 883-1131 9.37e-63

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 215.13  E-value: 9.37e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  883 PENKHKNRYINILAYDHSRVKLRplpGKDSK--HSDYINANYVDGY-----NKAKAYIATQGPLKSTFEDFWRMIWEQNT 955
Cdd:cd14606     16 PENKSKNRYKNILPFDHSRVILQ---GRDSNipGSDYINANYVKNQllgpdENAKTYIASQGCLEATVNDFWQMAWQENS 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  956 GIIVMITNLVEKGRRKCDQYWPTENSE-EYGNIIVTLKSTKIHACYTVRrfSIRNTKVKKGQKgnpkgrqnERVVIQYHY 1034
Cdd:cd14606     93 RVIVMTTREVEKGRNKCVPYWPEVGMQrAYGPYSVTNCGEHDTTEYKLR--TLQVSPLDNGEL--------IREIWHYQY 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1035 TQWPDMGVPEYALPVLTFVRRSSAAR--MPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDK---STVNVLGFLKHIRTQ 1109
Cdd:cd14606    163 LSWPDHGVPSEPGGVLSFLDQINQRQesLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKgldCDIDIQKTIQMVRAQ 242

                          250       260
                   ....*....|....*....|..
gi 2462591655 1110 RNYLVQTEEQYIFIHDALLEAI 1131
Cdd:cd14606    243 RSGMVQTEAQYKFIYVAIAQFI 264
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 889-1124 1.41e-60

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates.


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 207.07  E-value: 1.41e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  889 NRYINILAYDHSRVKLRPLPGkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKG 968
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAG--VPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  969 RRKCDQYWPTENS--EEYGNIIVTLKSTKIHACYTVRRFSIRntkvKKGqkgnpkgrqNERVVIQYHYTQWPDMGVPEYA 1046
Cdd:cd14616     79 RIRCHQYWPEDNKpvTVFGDIVITKLMEDVQIDWTIRDLKIE----RHG---------DYMMVRQCNFTSWPEHGVPESS 145

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462591655 1047 LPVLTFVRRSSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1124
Cdd:cd14616    146 APLIHFVKLVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 916-1130 1.54e-60

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 206.80  E-value: 1.54e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  916 DYINANYVD----GYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTEN-SEEYGNIIVT 990
Cdd:cd14541      1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGeTMQFGNLQIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  991 LKSTKIHACYTVRRFSIRNTKVKKgqkgnpkgrqnERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPETGPVLVH 1070
Cdd:cd14541     81 CVSEEVTPSFAFREFILTNTNTGE-----------ERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVH 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1071 CSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEA 1130
Cdd:cd14541    150 CSAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 875-1127 2.41e-60

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 207.38  E-value: 2.41e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  875 ITAEHSNHPENKHKNRYINILAYDHSRVKLRPlPGKDSKHSDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWEQ 953
Cdd:cd14612      5 VSPEELDIPGHASKDRYKTILPNPQSRVCLRR-AGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQE 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  954 NTGIIVMITNLVEKgRRKCDQYWPtENSEEYGNIIVTLKSTKIHACYTVRRFSIrntkvkkgqkgnpKGRQNERVVIQYH 1033
Cdd:cd14612     84 ECPIIVMITKLKEK-KEKCVHYWP-EKEGTYGRFEIRVQDMKECDGYTIRDLTI-------------QLEEESRSVKHYW 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1034 YTQWPDMGVPEYALPVLTFVRRSSAARM--PETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRN 1111
Cdd:cd14612    149 FSSWPDHQTPESAGPLLRLVAEVEESRQtaASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRG 228

                          250
                   ....*....|....*.
gi 2462591655 1112 YLVQTEEQYIFIHDAL 1127
Cdd:cd14612    229 GMIQTSEQYQFLHHTL 244
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 860-1129 5.76e-60

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 206.99  E-value: 5.76e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  860 SEDFEEVQRCTA----DMNITAEHSNHPENKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIAT 935
Cdd:cd14603      1 AGEFSEIRACSAafkaDYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLL--QEEGHSDYINANFIKGVDGSRAYIAT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  936 QGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP-TENSEEYGNIIVT-LKSTKIHACYTVRRFSIrntkvk 1013
Cdd:cd14603     79 QGPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAqEQEPLQTGPFTITlVKEKRLNEEVILRTLKV------ 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1014 kgqkgnpKGRQNERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPETGPVLVHCSAGVGRTGTYIVIDS-----ML 1088
Cdd:cd14603    153 -------TFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYvrqllLT 225

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2462591655 1089 QQIKDKstVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1129
Cdd:cd14603    226 QRIPPD--FSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 880-1129 8.44e-60

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 207.19  E-value: 8.44e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  880 SNHPENKHKNRYINILAYDHSRVKLRplpgkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIV 959
Cdd:cd14608     20 AKLPKNKNRNRYRDVSPFDHSRIKLH------QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVV 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  960 MITNLVEKGRRKCDQYWPTENSEEY----GNIIVTLKSTKIHACYTVRRFSIRNTKVkkgqkgnpkgrQNERVVIQYHYT 1035
Cdd:cd14608     94 MLNRVMEKGSLKCAQYWPQKEEKEMifedTNLKLTLISEDIKSYYTVRQLELENLTT-----------QETREILHFHYT 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1036 QWPDMGVPEYALPVLTFV--RRSSAARMPETGPVLVHCSAGVGRTGTYIVIDS---MLQQIKDKSTVNVLGFLKHIRTQR 1110
Cdd:cd14608    163 TWPDFGVPESPASFLNFLfkVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFR 242

                          250
                   ....*....|....*....
gi 2462591655 1111 NYLVQTEEQYIFIHDALLE 1129
Cdd:cd14608    243 MGLIQTADQLRFSYLAVIE 261
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 841-1135 1.85e-59

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 206.71  E-value: 1.85e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  841 VKQFVKHIGELYSNNQHG---FSEDFEEVQRCTADM-------NITAEHSnhpENKHKNRYINILAYDHSRVKLR-PLPG 909
Cdd:cd14604      6 LKKFIERVQAMKSTDHNGednFASDFMRLRRLSTKYrtekiypTATGEKE---ENVKKNRYKDILPFDHSRVKLTlKTSS 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  910 KDSkhsDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPT--ENSEEYGNI 987
Cdd:cd14604     83 QDS---DYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLygEEPMTFGPF 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  988 IVTLKSTKIHACYTVRRFSIRntkvkkgqkgnpkgRQNE-RVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPETGP 1066
Cdd:cd14604    160 RISCEAEQARTDYFIRTLLLE--------------FQNEtRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVP 225

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462591655 1067 VLVHCSAGVGRTGTYIVID---SMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEaILGKE 1135
Cdd:cd14604    226 ICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ-LFEKQ 296
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
 80-359 2.72e-59

Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues. This subgroup, restricted to animals, contains isozyme IV and similar proteins such as mouse CA XV. Isozymes IV is attached to membranes via a glycosylphosphatidylinositol (GPI) tail. In mammals, Isozyme IV plays crucial roles in kidney and lung function, amongst others. This subgroup also contains the dual domain CA from the giant clam, Tridacna gigas. T. gigas CA plays a role in the movement of inorganic carbon from the surrounding seawater to the symbiotic algae found in the clam's tissues. CA XV is expressed in several species but not in humans or chimps. Similar to isozyme CA IV, CA XV attaches to membranes via a GPI tail.


Pssm-ID: 239391  Cd Length: 234  Bit Score: 204.04  E-value: 2.72e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   80 GRHQSPIDILDQYARVGEEYQELQLDGFDNESSNKtWMKNTGKTVAILLKDDYFVSGAGLPGRFKAEKVEFHWGhSNGSA 159
Cdd:cd03117      1 GKRQSPINIVTKKVQYDENLTPFTFTGYDDTTTNW-TITNNGHTVQVTLPDGAKISGGGLPGTYKALQFHFHWG-SNGSP 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  160 GSEHSINGRRFPVEaedacrgdiMLMLSqgmrfillglKKEqfeerkswtTYQSMQIFFYNPDDfdsfqtaisenriIGA 239
Cdd:cd03117     79 GSEHTIDGERYPME---------LHIVH----------IKE---------SYNSLLEALKDSDG-------------LAV 117

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  240 MAIFFQVSPRDNSALDPIIHGLKGVVHHEKETFLDPFVLRDLLP-ASLGSYYRYTGSLTTPPCSEIVEWIVFRRPVPISY 318
Cdd:cd03117    118 LGFFIEEGEEENTNFDPLISALSNIPQKGGSTNLTPFSLRSLLPsVLLTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISR 197

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2462591655  319 HQLEAFYSI--FTTEQQDHVKsveylrNNFRPQQRLHDRVVSK 359
Cdd:cd03117    198 AQLDAFSTVlfFDTDNGQPMV------NNFRPVQPLNGRVVYA 234
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 888-1127 3.04e-59

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 204.71  E-value: 3.04e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  888 KNRYINILAYDHSRVKLRPlPGKDSKHSDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVE 966
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTS-PDQDDPLSSYINANYIRGYGgEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEE 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  967 KGRrKCDQYWPtENSEEYGNIIVTLKSTkIHAcytvRRFSIRNTKVKKGQKgnpkgrqnERVVIQYHYTQWPDMGVPEYA 1046
Cdd:cd14613    107 MNE-KCTEYWP-EEQVTYEGIEITVKQV-IHA----DDYRLRLITLKSGGE--------ERGLKHYWYTSWPDQKTPDNA 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1047 LPVLTFVRRSSAARM---PETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFI 1123
Cdd:cd14613    172 PPLLQLVQEVEEARQqaePNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFV 251


                   ....
gi 2462591655 1124 HDAL 1127
Cdd:cd14613    252 HHVL 255
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1216-1416 6.82e-59

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 201.36  E-value: 6.82e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFV-YWPSR-EESMNCEAFTVTLISK 1293
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCErYWPEEgGKPLEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1294 DRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAP--ISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGM 1371
Cdd:cd00047     81 EEL-----SDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPssPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGT 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2462591655 1372 LCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYK 1416
Cdd:cd00047    156 FIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 917-1127 8.22e-59

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 201.34  E-value: 8.22e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKI 996
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  997 HACYTVRRFSIRNTKVKKgqkgnpkgrqnERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPE-TGPVLVHCSAGV 1075
Cdd:cd14552     81 YEDYTLRDFLVTKGKGGS-----------TRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSgNHPITVHCSAGA 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462591655 1076 GRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDAL 1127
Cdd:cd14552    150 GRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 863-1128 1.14e-58

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 203.54  E-value: 1.14e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  863 FEEVQRCTADMNITAehSNHPENKHKNRYINILAYDHSRVKLRplpGKDskhsDYINANYVD----GYNKAKAYIATQGP 938
Cdd:cd14600     20 FEQLYRKKPGLAITC--AKLPQNMDKNRYKDVLPYDATRVVLQ---GNE----DYINASYVNmeipSANIVNKYIATQGP 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  939 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP-TENSEEYGNIIVTLKSTKIHACYTVRRFSIrnTKVKKGQk 1017
Cdd:cd14600     91 LPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPdPPDVMEYGGFRVQCHSEDCTIAYVFREMLL--TNTQTGE- 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1018 gnpkgrqnERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMpETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTV 1097
Cdd:cd14600    168 --------ERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRV-ENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPV 238

                          250       260       270
                   ....*....|....*....|....*....|.
gi 2462591655 1098 NVLGFLKHIRTQRNYLVQTEEQYIFIHDALL 1128
Cdd:cd14600    239 YPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 269
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 917-1131 2.07e-58

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 200.29  E-value: 2.07e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYV--DGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPtENSEE----YGNIIVT 990
Cdd:cd14538      1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWP-DSLNKplicGGRLEVS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  991 LKSTKIHACYTVRRFSIRNTKVKKgqkgnpkgrqnERVVIQYHYTQWPDMGVPEYALPVLTFVRRssAARMPETGPVLVH 1070
Cdd:cd14538     80 LEKYQSLQDFVIRRISLRDKETGE-----------VHHITHLNFTTWPDHGTPQSADPLLRFIRY--MRRIHNSGPIVVH 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462591655 1071 CSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 1131
Cdd:cd14538    147 CSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 917-1124 1.70e-57

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), type 18 (PTPN18) and type 12 (PTPN12) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. TPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling.


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 197.65  E-value: 1.70e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEE--YGNIIVTLKST 994
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlqFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  995 KihacYTVRRFSIRNTKVKKGQKgnpkgrqnERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPETGPVLVHCSAG 1074
Cdd:cd14542     81 K----RVGPDFLIRTLKVTFQKE--------SRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAG 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462591655 1075 VGRTGTYIVID---SMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1124
Cdd:cd14542    149 CGRTGTICAIDyvwNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 850-1131 1.80e-57

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 200.67  E-value: 1.80e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  850 ELYSNNQHGFSEDFEEVQRCTADMNITAEhSNHPENKHKNRYINILAYDHSRVKLRplpGKDSK-HSDYINANYV-DGYN 927
Cdd:cd14610     10 EDHLKNKNRLEKEWEALCAYQAEPNATNV-AQREENVQKNRSLAVLPYDHSRIILK---AENSHsHSDYINASPImDHDP 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  928 KAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHaC--YTVRRF 1005
Cdd:cd14610     86 RNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIW-CedFLVRSF 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1006 SIRNTKVkkgqkgnpkgrqNE-RVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPETGPVLVHCSAGVGRTGTYIVI 1084
Cdd:cd14610    165 YLKNLQT------------NEtRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILI 232

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2462591655 1085 DSMLQQI-KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 1131
Cdd:cd14610    233 DMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEV 280
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 885-1131 6.36e-57

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 199.11  E-value: 6.36e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  885 NKHKNRYINILAYDHSRVKLRPlpGKDSKHSDYINAN-YVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITN 963
Cdd:cd14609     42 NVKKNRNPDFVPYDHARIKLKA--ESNPSRSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTP 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  964 LVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHaC--YTVRRFSIRNTKVkkgqkgnpkgrQNERVVIQYHYTQWPDMG 1041
Cdd:cd14609    120 LVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIW-CedFLVRSFYLKNVQT-----------QETRTLTQFHFLSWPAEG 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1042 VPEYALPVLTFVRRSSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQI-KDKSTVNVLGFLKHIRTQRNYLVQTEEQY 1120
Cdd:cd14609    188 IPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGMVRTKDQF 267

                          250
                   ....*....|.
gi 2462591655 1121 IFIHDALLEAI 1131
Cdd:cd14609    268 EFALTAVAEEV 278
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 880-1127 1.22e-56

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 197.11  E-value: 1.22e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  880 SNHPENKHKNRYINILAYDHSRVKLRplpgkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIV 959
Cdd:cd14607     19 AKYPENRNRNRYRDVSPYDHSRVKLQ------NTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVV 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  960 MITNLVEKGRRKCDQYWPTENSEEYG----NIIVTLKSTKIHACYTVRRFSIRNtkVKKGQKgnpkgrqneRVVIQYHYT 1035
Cdd:cd14607     93 MLNRIVEKDSVKCAQYWPTDEEEVLSfketGFSVKLLSEDVKSYYTVHLLQLEN--INSGET---------RTISHFHYT 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1036 QWPDMGVPEYALPVLTFV--RRSSAARMPETGPVLVHCSAGVGRTGTYIVIDS--MLQQIKDKSTVNVLGFLKHIRTQRN 1111
Cdd:cd14607    162 TWPDFGVPESPASFLNFLfkVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTclVLMEKKDPDSVDIKQVLLDMRKYRM 241

                          250
                   ....*....|....*.
gi 2462591655 1112 YLVQTEEQYIFIHDAL 1127
Cdd:cd14607    242 GLIQTPDQLRFSYMAV 257
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 888-1124 1.83e-56

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type tyrosine-protein phosphatase-like R (PTPRR or R-PTP-R), also called protein-tyrosine phosphatase PCPTP1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRR is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. The human and mouse PTPRR gene produces multiple neuronal protein isoforms of varying sizes (in human, PTPPBS-alpha, beta, gamma and delta). All isoforms contain the KIM motif and the catalytic PTP domain. PTPRR-deficient mice show significant defects in fine motor coordination and balance skills that are reminiscent of a mild ataxia.


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 195.52  E-value: 1.83e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  888 KNRYINILAYDHSRVKLRPLPGKDSKhSDYINANYVDGY-NKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVE 966
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNSNDSL-STYINANYIRGYgGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  967 KGRrKCDQYWPtENSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgnpkGRQNeRVVIQYHYTQWPDMGVPEYA 1046
Cdd:cd14611     81 KNE-KCVLYWP-EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQ------------GSQS-RSVKHYWYTSWPDHKTPDSA 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1047 LPVLTFVRRSSAARM--PETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1124
Cdd:cd14611    146 QPLLQLMLDVEEDRLasPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 888-1129 1.89e-55

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 192.75  E-value: 1.89e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  888 KNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEK 967
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDED--SDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  968 GRRKCDQYW--PTENSEEYGNIIVTLKSTKIHACYTVRRFsirntKVKKGQKgnpkgrqnERVVIQYHYTQWPDMGVPEY 1045
Cdd:cd14602     79 GKKKCERYWaePGEMQLEFGPFSVTCEAEKRKSDYIIRTL-----KVKFNSE--------TRTIYQFHYKNWPDHDVPSS 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1046 ALPVLTFVRRSSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDK---STVNVLGFLKHIRTQRNYLVQTEEQYIF 1122
Cdd:cd14602    146 IDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQRPSLVQTKEQYEL 225


                   ....*..
gi 2462591655 1123 IHDALLE 1129
Cdd:cd14602    226 VYNAVIE 232
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 890-1129 3.74e-55

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 191.80  E-value: 3.74e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  890 RYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGR 969
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVKRGEEN--TDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  970 RKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKgqkgnpkgrqnERVVIQYHYTQWPDMGVPEYALPV 1049
Cdd:cd14623     79 EKCAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENK-----------SRQIRQFHFHGWPEVGIPSDGKGM 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1050 LTFVrRSSAARMPETG--PVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDAL 1127
Cdd:cd14623    148 INII-AAVQKQQQQSGnhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226


                   ..
gi 2462591655 1128 LE 1129
Cdd:cd14623    227 QE 228
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
 67-360 3.90e-55

Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Alpha CAs are mostly monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the secreted CA VI, which is found in saliva, for example, and the membrane proteins CA IX, XII, and XIV.


Pssm-ID: 239397 [Multi-domain]  Cd Length: 248  Bit Score: 192.52  E-value: 3.90e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   67 GPEHWVTSSVSCGGRHQSPIDILDQYARVGEEYQELQLDGFDNESSNKTWMKNTGKTVAILLKDDYFVSGaGLPGRFKAE 146
Cdd:cd03123      1 GEDHWPKKYPACGGKRQSPIDIQTDIVQFDPSLPPLELVGYDLPGTEEFTLTNNGHTVQLSLPPTMHIRG-GPGTEYTAA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  147 KVEFHWGHSNGSAGSEHSINGRRFPVEAedacrgdimlmlsqgmrfillglkkeqfeerkswttyqsmQIFFYNPDDFDS 226
Cdd:cd03123     80 QLHLHWGGRGSLSGSEHTIDGIRFAAEL----------------------------------------HIVHYNSDKYSS 119

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  227 FQTAISENRIIGAMAIFFQVSPRDNSALDPIIHGLKGVVHHEKETFLDPFVLRDLLPASLGSYYRYTGSLTTPPCSEIVE 306
Cdd:cd03123    120 FDEAADKPDGLAVLAILIEVGYPENTYYEKIISHLHEIKYKGQETTVPGFNVRELLPEDLSHYYRYEGSLTTPPCYESVL 199

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462591655  307 WIVFRRPVPISYHQLEAFY-SIFTTEQQDhvksveyLRNNFRPQQRLHDRVVSKS 360
Cdd:cd03123    200 WTVFRDPVTLSKEQLETLEnTLMDTHNKT-------LQNNYRATQPLNGRVVEAS 247
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 917-1129 6.05e-55

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 190.75  E-value: 6.05e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYVDGY--NKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEE----YGNIIVT 990
Cdd:cd14540      1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHdaltFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  991 LKSTKIHACYTVRRFSIRNTkvkkgqkgnPKGRqnERVVIQYHYTQWPDMGVPEYALPVLTF------VRRSS----AAR 1060
Cdd:cd14540     81 TKFSVSSGCYTTTGLRVKHT---------LSGQ--SRTVWHLQYTDWPDHGCPEDVSGFLDFleeinsVRRHTnqdvAGH 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591655 1061 MPETgPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1129
Cdd:cd14540    150 NRNP-PTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 916-1124 1.23e-52

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 183.67  E-value: 1.23e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  916 DYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTK 995
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  996 IHACYTVRRFSIRNTKVKKgqkgnpkgrqnERVVIQYHYTQWPDMGVPEYALPVLTFVrRSSAARMPETG--PVLVHCSA 1073
Cdd:cd14622     81 LLETISIRDFLVTYNQEKQ-----------TRLVRQFHFHGWPEIGIPAEGKGMIDLI-AAVQKQQQQTGnhPIVVHCSA 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462591655 1074 GVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1124
Cdd:cd14622    149 GAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 917-1131 2.93e-52

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 182.64  E-value: 2.93e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTK 995
Cdd:cd14546      1 YINASTIYDHDpRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  996 I-HACYTVRRFSIRNTKVkkgqkgnpkgrQNERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPETGPVLVHCSAG 1074
Cdd:cd14546     81 IwCDDYLVRSFYLKNLQT-----------SETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDG 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462591655 1075 VGRTGTYIVIDSMLQQI-KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 1131
Cdd:cd14546    150 AGRTGTYILIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEV 207
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1185-1419 4.49e-51

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 180.41  E-value: 4.49e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1185 CNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQ 1264
Cdd:cd14554      5 CNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLR 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1265 SLAEDE-FVYWPSrEESMNCEAFTVtliskDRLCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--F 1341
Cdd:cd14554     85 EMGREKcHQYWPA-ERSARYQYFVV-----DPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1342 ELINVIKE--EALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAML 1419
Cdd:cd14554    159 DFIGQVHKtkEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 884-1128 5.79e-51

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 180.03  E-value: 5.79e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  884 ENKHKNRYINILAYDHSRVKLrplpGKDSkhsDYINANYVD---GyNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVM 960
Cdd:cd14597      2 ENRKKNRYKNILPYDTTRVPL----GDEG---GYINASFIKmpvG-DEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAM 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  961 ITNLVEKGRRKCDQYWPtensEEYGNIIVTLKSTKIHACYT--VRRFSIRNTKVKKGQKGnpkgrqNERVVIQYHYTQWP 1038
Cdd:cd14597     74 MTQEVEGGKIKCQRYWP----EILGKTTMVDNRLQLTLVRMqqLKNFVIRVLELEDIQTR------EVRHITHLNFTAWP 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1039 DMGVPEYALPVLTFVrrSSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEE 1118
Cdd:cd14597    144 DHDTPSQPEQLLTFI--SYMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTED 221

                          250
                   ....*....|
gi 2462591655 1119 QYIFIHDALL 1128
Cdd:cd14597    222 QYIFCYQVIL 231
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1136-1424 3.09e-50

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type tyrosine-protein phosphatase-like D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 179.93  E-value: 3.09e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1136 TEVSSNQLHSYVNSILIPGVGGK-TRLEKQFKLVTQCNAKYVECFSAQKECNKEKNRNSSVVPSERARVGLAPLPGMKGT 1214
Cdd:cd14628      1 TEVPARNLYAYIQKLTQIETGENvTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1215 DYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWPSrEESMNCEAFTVtlisk 1293
Cdd:cd14628     81 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKcHQYWPA-ERSARYQYFVV----- 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1294 DRLCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVI--KEEALTRDGPTIVHDEYGAVSA 1369
Cdd:cd14628    155 DPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfIDFIGQVhkTKEQFGQDGPISVHCSAGVGRT 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462591655 1370 GMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAMLSLVST 1424
Cdd:cd14628    235 GVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGS 289
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 859-1129 8.53e-50

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 178.65  E-value: 8.53e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  859 FSEdFEEVQRCTADMNITAehSNHPENKHKNRYINILAYDHSRVKLrpLPGKDSkHSDYINANYVDGYNKAKA--YIATQ 936
Cdd:cd14599     15 FTE-YEQIPKKKADGVFTT--ATLPENAERNRIREVVPYEENRVEL--VPTKEN-NTGYINASHIKVTVGGEEwhYIATQ 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  937 GPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP----TENSEEYGNIIVTLKSTKIHACYtvrrfSIRNTKV 1012
Cdd:cd14599     89 GPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPklgsKHSSATYGKFKVTTKFRTDSGCY-----ATTGLKV 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1013 KKGQKGnpkgrqNERVVIQYHYTQWPDMGVPEYALPVLTF------VRRSSAARMPETG----PVLVHCSAGVGRTGTYI 1082
Cdd:cd14599    164 KHLLSG------QERTVWHLQYTDWPDHGCPEEVQGFLSYleeiqsVRRHTNSMLDSTKncnpPIVVHCSAGVGRTGVVI 237

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2462591655 1083 VIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1129
Cdd:cd14599    238 LTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 917-1124 2.09e-49

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 174.57  E-value: 2.09e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYV--DGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRR-KCDQYWPTE--NSEEYGNIIVTL 991
Cdd:cd17658      1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEenESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  992 KSTKIhacyTVRRFSIRNTKVKKGQKGNPKgrqneRVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARmPETGPVLVHC 1071
Cdd:cd17658     81 KKLKH----SQHSITLRVLEVQYIESEEPP-----LSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIP-PSAGPIVVHC 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462591655 1072 SAGVGRTGTYIVIDSMLQQI--KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1124
Cdd:cd17658    151 SAGIGRTGAYCTIHNTIRRIleGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 917-1125 9.39e-49

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 2.


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 172.58  E-value: 9.39e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPtENSEEYGNIIVTLKSTKI 996
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG-DEKKTYGDIEVELKDTEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  997 HACYTVRRFSIRNTKVKKgqkgnpkgrqnERVVIQYHYTQWPDMGVPEYALPVLTFVRR------SSAARMPETGPVLVH 1070
Cdd:cd14558     80 SPTYTVRVFEITHLKRKD-----------SRTVYQYQYHKWKGEELPEKPKDLVDMIKSikqklpYKNSKHGRSVPIVVH 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462591655 1071 CSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHD 1125
Cdd:cd14558    149 CSDGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
 67-360 1.29e-48

Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the membrane proteins CA XII and XIV.


Pssm-ID: 239400  Cd Length: 249  Bit Score: 173.87  E-value: 1.29e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   67 GPEHWVTSSVSCGGRHQSPIDILDQYARVGEEYQELQLDGFDNESSNKTWMKNTGKTVAILLKDDYFVSGagLPGRFKAE 146
Cdd:cd03126      1 GENSWPKKYPFCGGVAQSPIDIHTDILQYDSSLPPLEFHGYNVSGTEQFTLTNNGHTVQLSLPPTMHIGG--LPFKYTAS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  147 KVEFHWGHSNGSAGSEHSINGRRFPVEaedacrgdimlmlsqgmrfillglkkeqfeerkswttyqsMQIFFYNPDDFDS 226
Cdd:cd03126     79 QLHLHWGQRGSPEGSEHTISGKHFAAE----------------------------------------LHIVHYNSDKYPD 118

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  227 FQTAISENRIIGAMAIFFQVSPRdNSALDPIIHGLKGVVHHEKETFLDPFVLRDLLPASLGSYYRYTGSLTTPPCSEIVE 306
Cdd:cd03126    119 ISTAMNKSQGLAVLGILIEVGPF-NPSYEKIFSHLHEVKYKDQKVSVPGFNVQELLPKRLDEYYRYEGSLTTPPCYPSVL 197

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462591655  307 WIVFRRPVPISYHQLEAFY-SIFTTEQQDHVKSVeylrNNFRPQQRLHDRVVSKS 360
Cdd:cd03126    198 WTVFRNPVQISQEQLLALEtALYSTEEDESREMV----NNYRQVQPFNERLVFAS 248
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1136-1424 1.83e-48

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 174.92  E-value: 1.83e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1136 TEVSSNQLHSYVNSI--LIPGvGGKTRLEKQFKLVTQCNAKYVECFSAQKECNKEKNRNSSVVPSERARVGLAPLPGMKG 1213
Cdd:cd14627      2 TEVPARNLYSYIQKLaqVEVG-EHVTGMELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1214 TDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWPSrEESMNCEAFTVtlis 1292
Cdd:cd14627     81 SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKcHQYWPA-ERSARYQYFVV---- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1293 kDRLCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVI--KEEALTRDGPTIVHDEYGAVS 1368
Cdd:cd14627    156 -DPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfIDFIGQVhkTKEQFGQDGPISVHCSAGVGR 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591655 1369 AGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAMLSLVST 1424
Cdd:cd14627    235 TGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLGS 290
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1136-1424 5.29e-48

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 173.76  E-value: 5.29e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1136 TEVSSNQLHSYVNSI-LIPGVGGKTRLEKQFKLVTQCNAKYVECFSAQKECNKEKNRNSSVVPSERARVGLAPLPGMKGT 1214
Cdd:cd14629      2 TEVPARNLYAHIQKLtQVPPGESVTAMELEFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1215 DYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWPSrEESMNCEAFTVtlisk 1293
Cdd:cd14629     82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKcHQYWPA-ERSARYQYFVV----- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1294 DRLCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVI--KEEALTRDGPTIVHDEYGAVSA 1369
Cdd:cd14629    156 DPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEgfIDFIGQVhkTKEQFGQDGPITVHCSAGVGRT 235

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462591655 1370 GMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAMLSLVST 1424
Cdd:cd14629    236 GVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGS 290
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 917-1125 1.08e-47

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 169.49  E-value: 1.08e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYVDGY-NKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTE--NSEEYGNIIVTLKS 993
Cdd:cd14539      1 YINASLIEDLtPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgQALVYGAITVSLQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  994 TKIHACYTVRRFSIrntkVKKGQKGNpkgrqneRVVIQYHYTQWPDMGVPEYALPVLTF---VRRSSAARMPETGPVLVH 1070
Cdd:cd14539     81 VRTTPTHVERIISI----QHKDTRLS-------RSVVHLQFTTWPELGLPDSPNPLLRFieeVHSHYLQQRSLQTPIVVH 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591655 1071 CSAGVGRTGTYIVIDSMLQQIK-DKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHD 1125
Cdd:cd14539    150 CSSGVGRTGAFCLLYAAVQEIEaGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 916-1129 1.94e-47

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 168.97  E-value: 1.94e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  916 DYINANYVDGYNKAKA----YIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP-TENSEEYGNIIVT 990
Cdd:cd14601      1 DYINANYINMEIPSSSiinrYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPePSGSSSYGGFQVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  991 LKSTKIHACYTVRRFSIrnTKVKKGQkgnpkgrqnERVVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPETGPVLVH 1070
Cdd:cd14601     81 CHSEEGNPAYVFREMTL--TNLEKNE---------SRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVH 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591655 1071 CSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1129
Cdd:cd14601    150 CSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
PHA02738 PHA02738
hypothetical protein; Provisional
 862-1127 3.37e-46

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 169.34  E-value: 3.37e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  862 DFEEVqrctadmnITAEH------------SNHPENKHKNRYINILAYDHSRVKLRplpgKDSKHSDYINANYVDGYNKA 929
Cdd:PHA02738    22 DCEEV--------ITREHqkvisekvdgtfNAEKKNRKLNRYLDAVCFDHSRVILP----AERNRGDYINANYVDGFEYK 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  930 KAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPT--ENSEEYGNIIVTLKSTKIHACYtvrrfsI 1007
Cdd:PHA02738    90 KKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDveQGSIRFGKFKITTTQVETHPHY------V 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1008 RNTKVKKgqkgnpKGRQNERVVIQYHYTQWPDMGVPEYALPVLTFV------RRSSAARMPETG-------PVLVHCSAG 1074
Cdd:PHA02738   164 KSTLLLT------DGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVlevrqcQKELAQESLQIGhnrlqppPIVVHCNAG 237

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462591655 1075 VGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDAL 1127
Cdd:PHA02738   238 LGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 864-1124 5.88e-46

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 168.26  E-value: 5.88e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  864 EEVQRCTADMNITAEHSNHPENKHKNRYINILAYDHSRVKLRplpGKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTF 943
Cdd:PHA02747    30 EHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILD---SGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETC 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  944 EDFWRMIWEQNTGIIVMIT-NLVEKGRRKCDQYW-PTENS--EEYGNIIVTLKSTkIHACYTVRRFSIRNtkvkkgqkgn 1019
Cdd:PHA02747   107 ADFWKAVWQEHCSIIVMLTpTKGTNGEEKCYQYWcLNEDGniDMEDFRIETLKTS-VRAKYILTLIEITD---------- 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1020 pKGRQNERVVIQYHYTQWPDMGVPEYALPVLTF------VRRSSAARMPET----GPVLVHCSAGVGRTGTYIVIDSMLQ 1089
Cdd:PHA02747   176 -KILKDSRKISHFQCSEWFEDETPSDHPDFIKFikiidiNRKKSGKLFNPKdallCPIVVHCSDGVGKTGIFCAVDICLN 254

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2462591655 1090 QIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIH 1124
Cdd:PHA02747   255 QLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 876-1132 1.31e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 167.90  E-value: 1.31e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  876 TAEHSNHPENKHKNRYINILAYDHSRVKL-----------------RPLPGKDSKHSDYINANYVDGYNKAKAYIATQGP 938
Cdd:PHA02746    42 TTNHFLKKENLKKNRFHDIPCWDHSRVVInaheslkmfdvgdsdgkKIEVTSEDNAENYIHANFVDGFKEANKFICAQGP 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  939 LKSTFEDFWRMIWEQNTGIIVMITNlVEKGRRKCDQYWPTENSEE--YGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgq 1016
Cdd:PHA02746   122 KEDTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWTKEEDSElaFGRFVAKILDIIEELSFTKTRLMITD------- 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1017 kgnpKGRQNERVVIQYHYTQWPDMGVPEYALPVLTFVRR--SSAARMPET--------GPVLVHCSAGVGRTGTYIVIDS 1086
Cdd:PHA02746   194 ----KISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKvnEEQAELIKQadndpqtlGPIVVHCSAGIGRAGTFCAIDN 269

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2462591655 1087 MLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 1132
Cdd:PHA02746   270 ALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAII 315
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 917-1131 3.47e-45

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 162.22  E-value: 3.47e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYVDGYNKAKA--YIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE--EYGNIIVTLK 992
Cdd:cd14596      1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEpmELENYQLRLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  993 STKIhacytVRRFSIRNTKVKKGQKGnpkgrqNERVVIQYHYTQWPDMGVPEYALPVLTFVRrsSAARMPETGPVLVHCS 1072
Cdd:cd14596     81 NYQA-----LQYFIIRIIKLVEKETG------ENRLIKHLQFTTWPDHGTPQSSDQLVKFIC--YMRKVHNTGPIVVHCS 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591655 1073 AGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 1131
Cdd:cd14596    148 AGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
879-1123 6.09e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 158.72  E-value: 6.09e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  879 HSNHPENKHKNRYINILAYDHSRVklrplpGKDSKhsdYINANYVDGYNKaKAYIATQGPLKSTFEDFWRMIWEQNTGII 958
Cdd:COG5599     36 YLQNINGSPLNRFRDIQPYKETAL------RANLG---YLNANYIQVIGN-HRYIATQYPLEEQLEDFFQMLFDNNTPVL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  959 VMITNLVE--KGRRKCDQYWPTenSEEYGNIIVTLKSTKIHACYTvrRFSIRNTKVKKGQKGnpkgrQNERVVIQYHYTQ 1036
Cdd:COG5599    106 VVLASDDEisKPKVKMPVYFRQ--DGEYGKYEVSSELTESIQLRD--GIEARTYVLTIKGTG-----QKKIEIPVLHVKN 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1037 WPDMGVP--EYALPVLTFVRRSSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKS--TVNVLGFLKHIRTQRNY 1112
Cdd:COG5599    177 WPDHGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRNG 256

                          250
                   ....*....|..
gi 2462591655 1113 -LVQTEEQYIFI 1123
Cdd:COG5599    257 gMVQTSEQLDVL 268
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1216-1415 1.72e-42

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 154.49  E-value: 1.72e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFVYWPsrEESMNCEA-FTVTLISKD 1294
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQSCPQYWP--DEGSGTYGpIQVEFVSTT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1295 RlclsnEEQIIIHDFILEAT---QDDYVLeVRHFQCPKWP-NPDAPIS--STFELIN-VIKEEALTRDGPTIVHDEYGAV 1367
Cdd:cd14556     79 I-----DEDVISRIFRLQNTtrpQEGYRM-VQQFQFLGWPrDRDTPPSkrALLKLLSeVEKWQEQSGEGPIVVHCLNGVG 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2462591655 1368 SAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIY 1415
Cdd:cd14556    153 RSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 917-1129 5.93e-42

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 153.59  E-value: 5.93e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANY--VDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWP----TENSEEYGNIIVT 990
Cdd:cd14598      1 YINASHikVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsRHNTVTYGRFKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  991 LKSTKIHACYTVRRFSIRNtkVKKGQkgnpkgrqnERVVIQYHYTQWPDMGVPEYALPVLTF------VRR---SSAARM 1061
Cdd:cd14598     81 TRFRTDSGCYATTGLKIKH--LLTGQ---------ERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsVRRhtnSTIDPK 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462591655 1062 PETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1129
Cdd:cd14598    150 SPNPPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 884-1129 1.84e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 155.16  E-value: 1.84e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  884 ENKHKNRYINILAYDHSRVKLRPLPGKDskhsDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITN 963
Cdd:PHA02742    51 KNMKKCRYPDAPCFDRNRVILKIEDGGD----DFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITK 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  964 LVEKGRRKCDQYWpteNSEEYGNII---VTLKSTKIHacyTVRRFSIRNTKVKKGQKGNPKGRQNervviqYHYTQWPDM 1040
Cdd:PHA02742   127 IMEDGKEACYPYW---MPHERGKAThgeFKIKTKKIK---SFRNYAVTNLCLTDTNTGASLDIKH------FAYEDWPHG 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1041 GVPEYALPVLTFV----RRSSAARMPETG-------PVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQ 1109
Cdd:PHA02742   195 GLPRDPNKFLDFVlavrEADLKADVDIKGenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQ 274

                          250       260
                   ....*....|....*....|
gi 2462591655 1110 RNYLVQTEEQYIFIHDALLE 1129
Cdd:PHA02742   275 RHNCLSLPQQYIFCYFIVLI 294
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1216-1418 3.41e-41

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 150.88  E-value: 3.41e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWPSrEESMNCEAFTVTLiSKD 1294
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKcAQYWPE-DGSVSSGDITVEL-KDQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1295 RLClsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVI----KEEALTRDGPTIVHDEYGAVSAG 1370
Cdd:cd14552     79 TDY----EDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIP-DNGKGMIDLIaavqKQQQQSGNHPITVHCSAGAGRTG 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2462591655 1371 MLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAM 1418
Cdd:cd14552    154 TFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1191-1416 6.27e-41

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 150.58  E-value: 6.27e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1191 RNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLP---DNQSLA 1267
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTqcmEKGRVK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1268 EDEfvYWPSREESMNCEAFTVTLISKDRLclsneEQIIIHDFILEatQDDYVLEVRHFQCPKWPN---PDAPISstfeLI 1344
Cdd:cd14548     81 CDH--YWPFDQDPVYYGDITVTMLSESVL-----PDWTIREFKLE--RGDEVRSVRQFHFTAWPDhgvPEAPDS----LL 147

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462591655 1345 NVIKeeaLTRD------GPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYK 1416
Cdd:cd14548    148 RFVR---LVRDyikqekGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 917-1125 1.52e-40

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 148.71  E-value: 1.52e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMItNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKI 996
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSGTYGPIQVEFVSTTI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  997 HACYTVRRFSIRNTKvkkgqkgnpkgRQNE--RVVIQYHYTQWPDMG----VPEYALPVLTFVRRSSAARmpETGPVLVH 1070
Cdd:cd14556     80 DEDVISRIFRLQNTT-----------RPQEgyRMVQQFQFLGWPRDRdtppSKRALLKLLSEVEKWQEQS--GEGPIVVH 146

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462591655 1071 CSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHD 1125
Cdd:cd14556    147 CLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1184-1423 4.74e-39

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 146.00  E-value: 4.74e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1184 ECNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdn 1263
Cdd:cd14553      1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMM--- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1264 QSLAEDEFV----YWPSReESMNCEAFTVTLIskDRLCLSNeeqIIIHDFILEATQDDYVLEVRHFQCPKWPN---PDAP 1336
Cdd:cd14553     78 TKLEERSRVkcdqYWPTR-GTETYGLIQVTLL--DTVELAT---YTVRTFALHKNGSSEKREVRQFQFTAWPDhgvPEHP 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1337 iSSTFELINVIKEEALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVF-QVAKM---INLMrpgVFTDiEQYQ 1412
Cdd:cd14553    152 -TPFLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYgHVTCLraqRNYM---VQTE-DQYI 226

                          250
                   ....*....|.
gi 2462591655 1413 FIYKAMLSLVS 1423
Cdd:cd14553    227 FIHDALLEAVT 237
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1215-1418 7.17e-39

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 144.38  E-value: 7.17e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1215 DYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWPSrEESMNCEAFTVTlISK 1293
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKcVQYWPS-EGSVTHGEITIE-IKN 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1294 DRLClsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVI----KEEALTRDGPTIVHDEYGAVSA 1369
Cdd:cd14622     79 DTLL----ETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIP-AEGKGMIDLIaavqKQQQQTGNHPIVVHCSAGAGRT 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2462591655 1370 GMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAM 1418
Cdd:cd14622    154 GTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1029-1129 8.79e-39

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 140.19  E-value: 8.79e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  1029 VIQYHYTQWPDMGVPEYALPVLTFVR--RSSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKS-TVNVLGFLKH 1105
Cdd:smart00404    2 VKHYHYTGWPDHGVPESPDSILELLRavKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|....
gi 2462591655  1106 IRTQRNYLVQTEEQYIFIHDALLE 1129
Cdd:smart00404   82 LRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1029-1129 8.79e-39

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 140.19  E-value: 8.79e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  1029 VIQYHYTQWPDMGVPEYALPVLTFVR--RSSAARMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKS-TVNVLGFLKH 1105
Cdd:smart00012    2 VKHYHYTGWPDHGVPESPDSILELLRavKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|....
gi 2462591655  1106 IRTQRNYLVQTEEQYIFIHDALLE 1129
Cdd:smart00012   82 LRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1190-1422 3.28e-38

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 143.49  E-value: 3.28e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1190 NRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqsLAED 1269
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTN---CMEA 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1270 EFV----YWPSREESMNCEAFTVTLISKDRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELI- 1344
Cdd:cd14619     78 GRVkcehYWPLDYTPCTYGHLRVTVVSEEVM-----ENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVP-SSTDTLLa 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1345 --NVIKE--EALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAMLS 1420
Cdd:cd14619    152 frRLLRQwlDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231


                   ..
gi 2462591655 1421 LV 1422
Cdd:cd14619    232 FL 233
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1216-1415 6.21e-38

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 2.


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 141.38  E-value: 6.21e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQSLAEDEFVYWPsrEESMNCEAFTVTLISKD 1294
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTElKEGDQEQCAQYWG--DEKKTYGDIEVELKDTE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1295 rlclsNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVIKE---------EALTRDGPTIVHDEYG 1365
Cdd:cd14558     79 -----KSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELP-EKPKDLVDMIKSikqklpyknSKHGRSVPIVVHCSDG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1366 AVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIY 1415
Cdd:cd14558    153 SSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1190-1419 8.61e-38

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 141.88  E-value: 8.61e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1190 NRNSSVVPSERARVGLApLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAE- 1268
Cdd:cd14615      1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRt 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1269 --DEfvYWPSrEESMNCEAFTVTLISKDRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELIN- 1345
Cdd:cd14615     80 kcEE--YWPS-KQKKDYGDITVTMTSEIVL-----PEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVP-ETTDLLINf 150

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462591655 1346 --VIKE--EALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAML 1419
Cdd:cd14615    151 rhLVREymKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCAL 228
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1195-1418 1.50e-37

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 141.34  E-value: 1.50e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1195 VVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFV-Y 1273
Cdd:cd14623      5 IIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAqY 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1274 WPSrEESMNCEAFTVTLiSKDRLClsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVI----KE 1349
Cdd:cd14623     85 WPS-DGSVSYGDITIEL-KKEEEC----ESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIP-SDGKGMINIIaavqKQ 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591655 1350 EALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAM 1418
Cdd:cd14623    158 QQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 67-360 1.57e-37

Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Alpha CAs are strictly monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the membrane protein CA IX. CA IX is functionally implicated in tumor growth and survival. CA IX is mainly present in solid tumors and its expression in normal tissues is limited to the mucosa of alimentary tract. CA IX is a transmembrane protein with two extracellular domains: carbonic anhydrase and, a proteoglycan-like segment mediating cell-cell adhesion. There is evidence for an involvement of the MAPK pathway in the regulation of CA9 expression.


Pssm-ID: 239403  Cd Length: 247  Bit Score: 142.02  E-value: 1.57e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   67 GPEHWVTSSVSCGGRHQSPIDILDQYARVGEEYQELQLDGFDNESSNKTWMKNTGKTVAILLKDDYFVSGAglPGR-FKA 145
Cdd:cd03150      1 GQPPWPSVSPACAGRFQSPVDIRPHLVAFCPALRPLELLGFDLPPSPSLRLLNNGHTVQLSLPSGLRMALG--PGQeYRA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  146 EKVEFHWGhSNGSAGSEHSINGRRFPVEaedacrgdimlmlsqgmrfillglkkeqfeerkswttyqsMQIFFYNpDDFD 225
Cdd:cd03150     79 LQLHLHWG-AAGRPGSEHTVDGHRFPAE----------------------------------------IHVVHLS-TAFA 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  226 SFQTAISENRIIGAMAIFFQVSPRDNSALDPIIHGLKGVVHHEKETFLDPFVLRDLLPASLGSYYRYTGSLTTPPCSEIV 305
Cdd:cd03150    117 NLDEALGRPGGLAVLAAFLAEGLHENSAYEQLLSRLSEISEEESETVVPGLDVSALLPSDLSRYFRYEGSLTTPPCAQGV 196

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462591655  306 EWIVFRRPVPISYHQLEAFYSIFTTEQQdhvksvEYLRNNFRPQQRLHDRVVSKS 360
Cdd:cd03150    197 IWTVFNQTVRLSAKQLHTLSDSLWGPHD------SRLQLNFRATQPLNGRKIEAS 245
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
53-360 3.32e-37

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 140.79  E-value: 3.32e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   53 KASGDPYWAYSGAYGPEHWVTSSVS---CG-GRHQSPIDILDQyarVGEEYQELQldgFDNESSNKTwMKNTGKTVAILL 128
Cdd:COG3338     21 AAASAPHWSYEGETGPEHWGELSPEfatCAtGKNQSPIDIRTA---IKADLPPLK---FDYKPTPLE-IVNNGHTIQVNV 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  129 KDDYFVSGAGLpgRFKAEKVEFHwghsngsAGSEHSINGRRFPVEAedacrgdimlmlsqgmrfillglkkeQFEERksw 208
Cdd:COG3338     94 DPGSTLTVDGK--RYELKQFHFH-------TPSEHTINGKSYPMEA--------------------------HLVHK--- 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  209 ttyqsmqiffyNPDDfdsfQTAIsenriigaMAIFFQVSpRDNSALDPIIHGL---KGvvhhEKETFLDPFVLRDLLPAS 285
Cdd:COG3338    136 -----------DADG----ELAV--------VGVLFEEG-AENPALAKLWANLpleAG----EEVALDATIDLNDLLPED 187

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462591655  286 LgSYYRYTGSLTTPPCSEIVEWIVFRRPVPISYHQLEAFYSIFtteqqdhvksveylRNNFRPQQRLHDRVVSKS 360
Cdd:COG3338    188 R-SYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAFARLY--------------PNNARPVQPLNGRLILES 247
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1163-1418 4.15e-37

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 141.12  E-value: 4.15e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1163 KQFKLVTQCNAKYVECFS------AQKEcNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQH 1236
Cdd:cd14603      2 GEFSEIRACSAAFKADYVcstvagGRKE-NVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1237 PLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEF-VYWPSREESMNCEAFTVTLISKDRLclsNEEQIIihdFILEATQ 1315
Cdd:cd14603     81 PLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCeRYWAQEQEPLQTGPFTITLVKEKRL---NEEVIL---RTLKVTF 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1316 DDYVLEVRHFQCPKWPN---PDAPiSSTFELINVIKEEALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQ 1392
Cdd:cd14603    155 QKESRSVSHFQYMAWPDhgiPDSP-DCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFS 233

                          250       260
                   ....*....|....*....|....*....
gi 2462591655 1393 VAKMINLM---RPGVFTDIEQYQFIYKAM 1418
Cdd:cd14603    234 IFDVVLEMrkqRPAAVQTEEQYEFLYHTV 262
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1190-1419 4.41e-36

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 137.00  E-value: 4.41e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1190 NRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLP---DNQSL 1266
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTvgmENGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1267 AEDEfvYWPSREESMNCEAFTVTLISKdrlclSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPN---PDAPiSSTFEL 1343
Cdd:cd14618     81 LCDH--YWPSESTPVSYGHITVHLLAQ-----SSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDhgiPEST-SSLMAF 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462591655 1344 INVIKEE--ALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAML 1419
Cdd:cd14618    153 RELVREHvqATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
 67-357 1.62e-35

Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This sub-family includes bacterial carbonic anhydrase alpha, as well as plant enzymes such as tobacco nectarin III and yam dioscorin and, carbonic anhydrases from molluscs, such as nacrein, which are part of the organic matrix layer in shells. Other members of this family may be involved in maintaining pH balance, in facilitating transport of carbon dioxide or carbonic acid, or in sensing carbon dioxide levels in the environment. Dioscorin is the major storage protein of yam tubers and may play a role as an antioxidant. Tobacco Nectarin may play a role in the maintenace of pH and oxidative balance in nectar. Mollusc nacrein may participate in calcium carbonate crystal formation of the nacreous layer. This subfamily also includes three alpha carbonic anhydrases from Chlamydomonas reinhardtii (CAH 1-3). CAHs1-2 are localized in the periplasmic space. CAH1 faciliates the movement of carbon dioxide across the plasma membrane when the medium is alkaline. CAH3 is localized to the thylakoid lumen and provides CO2 to Rubisco.


Pssm-ID: 239398 [Multi-domain]  Cd Length: 216  Bit Score: 135.09  E-value: 1.62e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   67 GPEHWVTSSV---SCG-GRHQSPIDILDQYARVGeeyQELQLDgFDNESSNKTwMKNTGKTVAILLKDDyfVSGAGLPGR 142
Cdd:cd03124      1 GPEHWGNLDPefaLCAtGKNQSPIDITTKAVVSD---KLPPLN-YNYKPTSAT-LVNNGHTIQVNFEGN--GGTLTIDGE 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  143 fKAEKVEFHWgHSngsaGSEHSINGRRFPVEaedacrgdimlmlsqgmrfillglkkeqfeerkswttyqsMQIFFYNPD 222
Cdd:cd03124     74 -TYQLLQFHF-HS----PSEHLINGKRYPLE----------------------------------------AHLVHKSKD 107

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  223 DfdsfQTAIsenriigaMAIFFQVSPrDNSALDPIIHGLKGVVhhEKETFLDPFV-LRDLLPASLgSYYRYTGSLTTPPC 301
Cdd:cd03124    108 G----QLAV--------VAVLFEEGK-ENPFLKKILDNMPKKE--GTEVNLPAILdPNELLPESR-SYYRYEGSLTTPPC 171

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591655  302 SEIVEWIVFRRPVPISYHQLEAFysiftteqqdhvKSVEYLRNNfRPQQRLHDRVV 357
Cdd:cd03124    172 SEGVRWIVLKQPITISKEQLAKF------------RAAVYPNNA-RPVQPLNGREV 214
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 67-360 3.82e-35

Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the secreted CA VI, which is found in saliva.


Pssm-ID: 239399  Cd Length: 249  Bit Score: 134.91  E-value: 3.82e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   67 GPEHWVTSSVSCGGRHQSPIDILDQYARVGEEYQELQLDGFDNESSNKTwMKNTGKTVAILLKDDYFVSgAGLPGRFKAE 146
Cdd:cd03125      1 DESHWPEKYPACGGKRQSPIDIQRREVRFNPSLLQLELVGYEKEQGEFT-MTNNGHTVQIDLPPTMSIT-TGDGTVYTAV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  147 KVEFHWG-HSNGSAGSEHSINGRRFPVEAedacrgdimlmlsqgmrfillglkkeqfeerkswttyqsmQIFFYNpDDFD 225
Cdd:cd03125     79 QMHFHWGgRDSEISGSEHTIDGMRYVAEL----------------------------------------HIVHYN-SKYK 117

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  226 SFQTAISENRIIGAMAIFFQV-SPRDNSALDPIIHGLKGVVHHEKETFLDPFVLRDLLPASLGSYYRYTGSLTTPPCSEI 304
Cdd:cd03125    118 SYEEAKDKPDGLAVLAFLYKVgHYAENTYYSDFISKLAKIKYAGQTTTLTSLDVRDMLPENLHHYYTYQGSLTTPPCTEN 197

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591655  305 VEWIVFRRPVPISYHQLEafySIFTTEQQDHVKSveyLRNNFRPQQRLHDRVVSKS 360
Cdd:cd03125    198 VLWFVFDDPVTLSKTQIV---KLENTLMDHHNKT---IRNDYRRTQPLNHRVVEAN 247
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1180-1416 5.98e-35

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 135.18  E-value: 5.98e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1180 SAQKECNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVM 1259
Cdd:cd14543     23 CSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVM 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1260 LpdnQSLAEDEFV----YWPSREES-MNCEAFTVTLISKDrlclsNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPD 1334
Cdd:cd14543    103 T---TRVVERGRVkcgqYWPLEEGSsLRYGDLTVTNLSVE-----NKEHYKKTTLEIHNTETDESRQVTHFQFTSWPDFG 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1335 APiSSTFELIN----VIKEEAL------------TRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMIN 1398
Cdd:cd14543    175 VP-SSAAALLDflgeVRQQQALavkamgdrwkghPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMR 253

                          250
                   ....*....|....*...
gi 2462591655 1399 LMRPGVFTDIEQYQFIYK 1416
Cdd:cd14543    254 TQRAFSIQTPDQYYFCYK 271
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1179-1419 6.69e-35

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 134.25  E-value: 6.69e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1179 FSAQKECNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIV 1258
Cdd:cd14614      5 FAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIV 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1259 MLP---DNQSLAEDEfvYWPSREESMNCEAFTVTLISKdrlclSNEEQIIIHDFILeaTQDDYVLEVRHFQCPKWPNPDA 1335
Cdd:cd14614     85 MLTqcnEKRRVKCDH--YWPFTEEPVAYGDITVEMLSE-----EEQPDWAIREFRV--SYADEVQDVMHFNYTAWPDHGV 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1336 P----ISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQY 1411
Cdd:cd14614    156 PtanaAESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQY 235


                   ....*...
gi 2462591655 1412 QFIYKAML 1419
Cdd:cd14614    236 IFIHQCVQ 243
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1190-1415 2.97e-33

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 128.67  E-value: 2.97e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1190 NRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGY-YRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAE 1268
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1269 DEFVYWPSrEESMNCEAFTVTLISKDRlclsnEEQIIIHDFILEatqddYVLEVR---HFQCPKWPN---PDAPiSSTFE 1342
Cdd:cd14547     81 KCAQYWPE-EENETYGDFEVTVQSVKE-----TDGYTVRKLTLK-----YGGEKRylkHYWYTSWPDhktPEAA-QPLLS 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462591655 1343 LINVIKEEALTRD--GPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIY 1415
Cdd:cd14547    149 LVQEVEEARQTEPhrGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1184-1423 3.66e-33

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 130.16  E-value: 3.66e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1184 ECNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdn 1263
Cdd:cd14626     39 EVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMM--- 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1264 QSLAEDEFV----YWPSReESMNCEAFTVTLISKDRLCLSNeeqiiIHDFILEATQDDYVLEVRHFQCPKWPN---PDAP 1336
Cdd:cd14626    116 TRLEEKSRVkcdqYWPIR-GTETYGMIQVTLLDTVELATYS-----VRTFALYKNGSSEKREVRQFQFMAWPDhgvPEYP 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1337 iSSTFELINVIKEEALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYK 1416
Cdd:cd14626    190 -TPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHE 268


                   ....*..
gi 2462591655 1417 AMLSLVS 1423
Cdd:cd14626    269 ALLEAAT 275
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 917-1123 9.85e-33

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 126.28  E-value: 9.85e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGrrKCDQYWPT-ENSEEYGNIIVTLKSTK 995
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTkEKPLECETFKVTLSGED 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  996 IHAC-----YTVRRFSIRNTkvkkgqkgnpkgrQNERV--VIQYHYTQWPDMGVPEY-ALPVLTFVRRSSAARmpeTGPV 1067
Cdd:cd14550     79 HSCLsneirLIVRDFILEST-------------QDDYVleVRQFQCPSWPNPCSPIHtVFELINTVQEWAQQR---DGPI 142

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591655 1068 LVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFI 1123
Cdd:cd14550    143 VVHDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1180-1419 1.51e-32

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 128.24  E-value: 1.51e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1180 SAQKECNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVM 1259
Cdd:cd14633     34 SAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIM 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1260 LPDNQSLAEDEFV-YWPSREESMncEAFTVTLISKDRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPIS 1338
Cdd:cd14633    114 VTNLVEVGRVKCCkYWPDDTEIY--KDIKVTLIETELL-----AEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYH 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1339 ST--FELINVIKEEALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYK 1416
Cdd:cd14633    187 ATglLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHD 266


                   ...
gi 2462591655 1417 AML 1419
Cdd:cd14633    267 AIL 269
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1186-1419 1.64e-32

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 127.06  E-value: 1.64e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1186 NKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQS 1265
Cdd:cd14630      3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1266 LAEDEFV-YWPSREESMNceAFTVTLISKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FE 1342
Cdd:cd14630     83 VGRVKCVrYWPDDTEVYG--DIKVTLIETEPLA-----EYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATglLG 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462591655 1343 LINVIKEEALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAML 1419
Cdd:cd14630    156 FVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1190-1416 1.68e-32

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates.


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 126.56  E-value: 1.68e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1190 NRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdNQSLAED 1269
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVML--TQCFEKG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1270 EF---VYWPsrEESMNCEAFTVTLISKdrlcLSNEEQI--IIHDFILEaTQDDYVLeVRHFQCPKWPNPDAPiSSTFELI 1344
Cdd:cd14616     79 RIrchQYWP--EDNKPVTVFGDIVITK----LMEDVQIdwTIRDLKIE-RHGDYMM-VRQCNFTSWPEHGVP-ESSAPLI 149

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462591655 1345 NVIKEEALTRDG---PTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYK 1416
Cdd:cd14616    150 HFVKLVRASRAHdntPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1184-1423 9.08e-32

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 126.36  E-value: 9.08e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1184 ECNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVM---L 1260
Cdd:cd14625     45 EVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMmtkL 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1261 PDNQSLAEDEfvYWPSREESmNCEAFTVTLISKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST 1340
Cdd:cd14625    125 EEKSRIKCDQ--YWPSRGTE-TYGMIQVTLLDTIELA-----TFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPT 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1341 --FELINVIKEEALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAM 1418
Cdd:cd14625    197 pfLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276


                   ....*
gi 2462591655 1419 LSLVS 1423
Cdd:cd14625    277 LEAVA 281
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
 58-360 1.48e-31

Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This vertebrate subgroup comprises isozymes I, II, and III, which are cytoplasmic enzymes. CA I, for example, is expressed in erythrocyes of many vertebrates; CA II is the most active cytosolic isozyme; while it is being expressed nearly ubiquitously, it comprises 95% of the renal carbonic anhydrase and is required for renal acidification; CA III has been implicated in protection from the damaging effect of oxidizing agents in hepatocytes. CAXIII may play important physiological roles in several organs.


Pssm-ID: 239393 [Multi-domain]  Cd Length: 259  Bit Score: 124.86  E-value: 1.48e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   58 PYWAYSGAYGPEHWVTSSVSCGGRHQSPIDILDQYARVGEEYQELQLDGfdNESSNKTwMKNTGKTVAILLKDDY---FV 134
Cdd:cd03119      3 HHWGYDSHNGPEHWHELFPIAKGDRQSPIDIKTKDAKHDPSLKPLSVSY--DPATAKT-ILNNGHSFNVEFDDTDdrsVL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  135 SGAGLPGRFKAEKVEFHWGHSNGSaGSEHSINGRRFPVEaedacrgdimlmlsqgmrfillglkkeqfeerkswttyqsM 214
Cdd:cd03119     80 RGGPLTGSYRLRQFHFHWGSSDDH-GSEHTVDGVKYAAE----------------------------------------L 118

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  215 QIFFYNPDdFDSFQTAISENRIIGAMAIFFQVSpRDNSALDPIIHGLKGVVHHEKETFLDPFVLRDLLPASLgSYYRYTG 294
Cdd:cd03119    119 HLVHWNSK-YGSFGEAAKQPDGLAVVGVFLKVG-EANPELQKVLDALDSIKTKGKQAPFTNFDPSCLLPASL-DYWTYPG 195

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591655  295 SLTTPPCSEIVEWIVFRRPVPISYHQLEAFYSIFTTEQQDhvkSVEYLRNNFRPQQRLHDRVVSKS 360
Cdd:cd03119    196 SLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNAEGE---PPCPMVDNWRPPQPLKGRKVRAS 258
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1190-1416 4.07e-31

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 122.72  E-value: 4.07e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1190 NRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQSLAED 1269
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMV---TQCVEK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1270 EFV----YWPSREESMNCEAFTVTLISKDRLclsneEQIIIHDF-ILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELI 1344
Cdd:cd14617     78 GRVkcdhYWPADQDSLYYGDLIVQMLSESVL-----PEWTIREFkICSEEQLDAPRLVRHFHYTVWPDHGVP-ETTQSLI 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1345 NVIKEealTRD--------GPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYK 1416
Cdd:cd14617    152 QFVRT---VRDyinrtpgsGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
 80-357 3.88e-30

Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup contains carbonic anhydrase related proteins (CARPs) X and XI, which have been implicated in various biological processes of the central nervous system. CARPs are sequence similar to carbonic anhydrases. Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism. CARPs have lost conserved histidines involved in zinc binding and consequently their catalytic activity. CARP XI plays a role in the development of gastrointestinal stromal tumors.


Pssm-ID: 239395 [Multi-domain]  Cd Length: 256  Bit Score: 120.60  E-value: 3.88e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   80 GRHQSPIDILDQYARVGEEYQELQLDGfdNESSNKTwMKNTGKTVAILLKDDYFV--SGAGLPGRFKAEKVEFHWGHSNG 157
Cdd:cd03121     18 GRRQSPVDIEPSRLLFDPFLTPLRIDT--GRKVSGT-FYNTGRHVSFRPDKDPVVniSGGPLSYRYRLEEIRLHFGREDE 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  158 sAGSEHSINGRRFPVEaedacrgdimlmlsqgmrfillglkkeqfeerkswttyqsMQIFFYNPDDFDSFQTAISENRII 237
Cdd:cd03121     95 -QGSEHTVNGQAFPGE----------------------------------------VQLIHYNSELYPNFSEASKSPNGL 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  238 GAMAIFFQVSPRDNSALDPIIHGLKG--VVHHEKETFLDPFVLRDLLPASlGSYYRYTGSLTTPPCSEIVEWIVFRRPVP 315
Cdd:cd03121    134 VIVSLFVKIGETSNPELRRLTNRDTItsIRYKGDAYFLQDLSIELLLPET-DHYITYEGSLTSPGCHETVTWIILNKPIY 212

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2462591655  316 ISYHQLEAFYSIfTTEQQDHVKSveYLRNNFRPQQRLHDRVV 357
Cdd:cd03121    213 ITKEQMHSLRLL-SQNSPSQEKA--PMSPNFRPVQPLNNRPV 251
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1184-1423 3.94e-30

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 121.76  E-value: 3.94e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1184 ECNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVM---L 1260
Cdd:cd14624     45 EVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMmtkL 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1261 PDNQSLAEDEfvYWPSREESMNcEAFTVTLISKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST 1340
Cdd:cd14624    125 EERSRVKCDQ--YWPSRGTETY-GLIQVTLLDTVELA-----TYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPT 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1341 --FELINVIKEEALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAM 1418
Cdd:cd14624    197 pfLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276


                   ....*
gi 2462591655 1419 LSLVS 1423
Cdd:cd14624    277 LEAVT 281
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 917-1129 5.18e-30

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 118.97  E-value: 5.18e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLveKGRRKCDQYWPTENSEEYGNIIVTLKSTKI 996
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGPIQVEFVSADI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  997 HACYTVRRFSIRNtkVKKGQKGnpkgrqnERVVIQYHYTQWPDM-GVPEYALPVLTFVRRssAARMPET-----GPVLVH 1070
Cdd:cd14634     79 DEDIISRIFRICN--MARPQDG-------YRIVQHLQYIGWPAYrDTPPSKRSILKVVRR--LEKWQEQydgreGRTVVH 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591655 1071 CSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1129
Cdd:cd14634    148 CLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1189-1418 5.37e-30

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 120.35  E-value: 5.37e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1189 KNRNSSVVPSERARVGL-APLPGMKGTDYINASYIMGY-YRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSL 1266
Cdd:cd14613     28 KNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1267 AEDEFVYWPsrEESMNCEAFTVTLisKDRLClsnEEQIIIHDFILEATQDDYVLevRHFQCPKWPNPDAPISST--FELI 1344
Cdd:cd14613    108 NEKCTEYWP--EEQVTYEGIEITV--KQVIH---ADDYRLRLITLKSGGEERGL--KHYWYTSWPDQKTPDNAPplLQLV 178

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462591655 1345 NVIKE---EALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAM 1418
Cdd:cd14613    179 QEVEEarqQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1189-1418 6.75e-30

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 119.94  E-value: 6.75e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1189 KNRNSSVVPSERARVGL-APLPGMKGTDYINASYIMGYY-RSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSL 1266
Cdd:cd14612     18 KDRYKTILPNPQSRVCLrRAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKEK 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1267 AEDEFVYWPSREESMNceAFTVTlISKDRLClsneEQIIIHDFILEATQDDYvlEVRHFQCPKWPNPDAPIS--STFELI 1344
Cdd:cd14612     98 KEKCVHYWPEKEGTYG--RFEIR-VQDMKEC----DGYTIRDLTIQLEEESR--SVKHYWFSSWPDHQTPESagPLLRLV 168

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591655 1345 NVIKE--EALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAM 1418
Cdd:cd14612    169 AEVEEsrQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTL 244
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1194-1419 6.80e-30

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).


Pssm-ID: 350468 [Multi-domain]  Cd Length: 229  Bit Score: 119.28  E-value: 6.80e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1194 SVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FV 1272
Cdd:cd14620      3 NILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKcYQ 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1273 YWPSReesmNCEAF-TVTLISKDRLCLSNeeqIIIHDFILEATQDDYVLEVR-----HFQcpKWPNPDAPIS--STFELI 1344
Cdd:cd14620     83 YWPDQ----GCWTYgNIRVAVEDCVVLVD---YTIRKFCIQPQLPDGCKAPRlvtqlHFT--SWPDFGVPFTpiGMLKFL 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462591655 1345 NVIKEEALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAML 1419
Cdd:cd14620    154 KKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
 80-360 1.12e-29

Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This vertebrate subgroup comprises isozyme VII. CA VII is the most active cytosolic enzyme after CA II, and may be highly expressed in the brain. Human CA VII may be a target of antiepileptic sulfonamides/sulfamates.


Pssm-ID: 239402  Cd Length: 236  Bit Score: 118.78  E-value: 1.12e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   80 GRHQSPIDILDQYARVGEEYQELQLDgFDNESSNKtwMKNTGKTVAILLkDDY----FVSGAGLPGRFKAEKVEFHWGhS 155
Cdd:cd03149      1 GNRQSPIDIVSSEAVYDPKLKPLSLS-YDPCTSLS--ISNNGHSVMVEF-DDSddktVITGGPLENPYRLKQFHFHWG-A 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  156 NGSAGSEHSINGRRFPVEaedacrgdimlmlsqgmrfillglkkeqfeerkswttyqsMQIFFYNPDDFDSFQTAISENR 235
Cdd:cd03149     76 KHGSGSEHTVDGKTFPSE----------------------------------------LHLVHWNAKKYKSFGEAAAAPD 115

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  236 IIGAMAIFFQVSpRDNSALDPIIHGLKGVVHHEKETFLDPFVLRDLLPASLgSYYRYTGSLTTPPCSEIVEWIVFRRPVP 315
Cdd:cd03149    116 GLAVLGVFLETG-DEHPGLNRLTDALYMVRFKGTKAQFLDFNPKCLLPKSL-DYWTYPGSLTTPPLNESVTWIVLKEPIP 193

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2462591655  316 ISYHQLEAFYS-IFTTEQQDHVKSVeylrNNFRPQQRLHDRVVSKS 360
Cdd:cd03149    194 VSEKQMGKFRElLFTSEEDQRNHMV----NNFRPPQPLKGRTVRAS 235
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1189-1421 1.16e-29

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 118.79  E-value: 1.16e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1189 KNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMlpdnqslAE 1268
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVM-------AC 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1269 DEFV--------YWP-SREESMNCEAFTVTLISKDrlclsNEEQIIIHdfILEATQDDYVLEVRHFQCPKWPNPDAP--I 1337
Cdd:cd14602     74 MEFEmgkkkcerYWAePGEMQLEFGPFSVTCEAEK-----RKSDYIIR--TLKVKFNSETRTIYQFHYKNWPDHDVPssI 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1338 SSTFELINVIKEEALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLM---RPGVFTDIEQYQFI 1414
Cdd:cd14602    147 DPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMrtqRPSLVQTKEQYELV 226


                   ....*..
gi 2462591655 1415 YKAMLSL 1421
Cdd:cd14602    227 YNAVIEL 233
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1186-1422 1.68e-29

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG has four splicing isoforms: three transmembrane isoforms, PTPRG-A, B, and C, and one secretory isoform, PTPRG-S, which are expressed in many tissues including the brain. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 119.37  E-value: 1.68e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1186 NKEKNRNSSVVPSERARVGLAPLPGM--KGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDn 1263
Cdd:cd17667     27 NKHKNRYINILAYDHSRVKLRPLPGKdsKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITN- 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1264 qsLAE------DEfvYWPSrEESMNCEAFTVTLIS-KDRLCLSneeqiiIHDFILEATQDDYVLE-----------VRHF 1325
Cdd:cd17667    106 --LVEkgrrkcDQ--YWPT-ENSEEYGNIIVTLKStKIHACYT------VRRFSIRNTKVKKGQKgnpkgrqnertVIQY 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1326 QCPKWPNPDAPISSTFELINVIKEEA--LTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPG 1403
Cdd:cd17667    175 HYTQWPDMGVPEYALPVLTFVRRSSAarTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNY 254

                          250
                   ....*....|....*....
gi 2462591655 1404 VFTDIEQYQFIYKAMLSLV 1422
Cdd:cd17667    255 LVQTEEQYIFIHDALLEAI 273
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1216-1415 1.95e-29

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 117.35  E-value: 1.95e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYI-MGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVML-PDNQSLAEDEFVYWPSREESMNCEAFTVTLISK 1293
Cdd:cd18533      1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLtPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1294 DRLclsNEEQIIIHDFILeATQDDYVLEVRHFQCPKWPNPDAP--ISSTFELINVIKE--EALTRDGPTIVHdeygaVSA 1369
Cdd:cd18533     81 EEN---DDGGFIVREFEL-SKEDGKVKKVYHIQYKSWPDFGVPdsPEDLLTLIKLKRElnDSASLDPPIIVH-----CSA 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462591655 1370 GM-----LCALTTLSQQLEN--------ENAVDVfqVAKMINLM---RPGVFTDIEQYQFIY 1415
Cdd:cd18533    152 GVgrtgtFIALDSLLDELKRglsdsqdlEDSEDP--VYEIVNQLrkqRMSMVQTLRQYIFLY 211
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1158-1418 3.23e-29

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 119.01  E-value: 3.23e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1158 KTRLEKQFKLVTQCNAKYVECFSAQKECNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGY-YRSNEFIITQH 1236
Cdd:cd14610     16 KNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHdPRNPAYIATQG 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1237 PLPHTTKDFWRMIWDHNAQIIVML-PDNQSLAEDEFVYWPSrEESMNCEAFTVTLISKDRLClsneEQIIIHDFILEATQ 1315
Cdd:cd14610     96 PLPATVADFWQMVWESGCVVIVMLtPLAENGVKQCYHYWPD-EGSNLYHIYEVNLVSEHIWC----EDFLVRSFYLKNLQ 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1316 DDYVLEVRHFQCPKWPNPDAPiSSTFELINV---IKEEALTRDGPTIVHDEYGAVSAGMLCAL-TTLSQQLENENAVDVF 1391
Cdd:cd14610    171 TNETRTVTQFHFLSWNDQGVP-ASTRSLLDFrrkVNKCYRGRSCPIIVHCSDGAGRSGTYILIdMVLNKMAKGAKEIDIA 249

                          250       260
                   ....*....|....*....|....*..
gi 2462591655 1392 QVAKMINLMRPGVFTDIEQYQFIYKAM 1418
Cdd:cd14610    250 ATLEHLRDQRPGMVQTKEQFEFALTAV 276
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1216-1419 4.52e-29

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 116.17  E-value: 4.52e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFV-YWPSREESMNceAFTVTLISKD 1294
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSrYWPDDTEVYG--DIKVTLVETE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1295 RLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPTIVHDEYGAVSAGML 1372
Cdd:cd14555     79 PLA-----EYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATglLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCY 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2462591655 1373 CALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAML 1419
Cdd:cd14555    154 IVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1158-1418 7.01e-29

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 117.83  E-value: 7.01e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1158 KTRLEKQFKLVTQCNAKYVECFSAQKECNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGY-YRSNEFIITQH 1236
Cdd:cd14609     14 RDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIEHdPRMPAYIATQG 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1237 PLPHTTKDFWRMIWDHNAQIIVMLpdnQSLAEDEFV----YWPSREESMNcEAFTVTLISKDRLClsneEQIIIHDFILE 1312
Cdd:cd14609     94 PLSHTIADFWQMVWENGCTVIVML---TPLVEDGVKqcdrYWPDEGSSLY-HIYEVNLVSEHIWC----EDFLVRSFYLK 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1313 ATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINV---IKEEALTRDGPTIVHDEYGAVSAGMLCAL-TTLSQQLENENAV 1388
Cdd:cd14609    166 NVQTQETRTLTQFHFLSWPAEGIP-SSTRPLLDFrrkVNKCYRGRSCPIIVHCSDGAGRTGTYILIdMVLNRMAKGVKEI 244

                          250       260       270
                   ....*....|....*....|....*....|
gi 2462591655 1389 DVFQVAKMINLMRPGVFTDIEQYQFIYKAM 1418
Cdd:cd14609    245 DIAATLEHVRDQRPGMVRTKDQFEFALTAV 274
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1178-1419 7.56e-29

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350469 [Multi-domain]  Cd Length: 296  Bit Score: 118.20  E-value: 7.56e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1178 CFSAQKECNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQII 1257
Cdd:cd14621     44 CEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATI 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1258 VMLPDNQSLAEDEFV-YWPSReesmNCEAFTVTLIS-KDRLCLSNeeqIIIHDFILEATQDDYVLE----VRHFQCPKWP 1331
Cdd:cd14621    124 VMVTNLKERKECKCAqYWPDQ----GCWTYGNIRVSvEDVTVLVD---YTVRKFCIQQVGDVTNKKpqrlITQFHFTSWP 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1332 NPDAPIS--STFELINVIKEEALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIE 1409
Cdd:cd14621    197 DFGVPFTpiGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDM 276

                          250
                   ....*....|
gi 2462591655 1410 QYQFIYKAML 1419
Cdd:cd14621    277 QYVFIYQALL 286
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1216-1419 9.04e-29

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 115.12  E-value: 9.04e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSlAEDEFVYWPsrEESMNCEA-FTVTLISKD 1294
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDA-AQLCMQYWP--EKTSCCYGpIQVEFVSAD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1295 RlclsnEEQIIIHDFI---LEATQDDYVLeVRHFQCPKWPN-PDAPIS--STFELINVI---KEEALTRDGPTIVHDEYG 1365
Cdd:cd14634     78 I-----DEDIISRIFRicnMARPQDGYRI-VQHLQYIGWPAyRDTPPSkrSILKVVRRLekwQEQYDGREGRTVVHCLNG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462591655 1366 AVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAML 1419
Cdd:cd14634    152 GGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVAL 205
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1216-1415 2.64e-28

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 113.60  E-value: 2.64e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqsLAE------DEfvYWPSrEESMNCEAFTVT 1289
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITN---LVErgrrkcDQ--YWPK-EGTETYGNIQVT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1290 LISKD--------RLCLSNEEqiiihdfILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVIKEEALTRD---GPT 1358
Cdd:cd14549     75 LLSTEvlatytvrTFSLKNLK-------LKKVKGRSSERVVYQYHYTQWPDHGVP-DYTLPVLSFVRKSSAANPpgaGPI 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462591655 1359 IVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMI----NLMrpgVFTDiEQYQFIY 1415
Cdd:cd14549    147 VVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIrtqrNYL---VQTE-EQYIFIH 203
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1216-1416 2.81e-28

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), type 18 (PTPN18) and type 12 (PTPN12) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. TPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling.


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 113.67  E-value: 2.81e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFV-YWP-SREESMNCEAFTVTLISK 1293
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCErYWPeEGEEQLQFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1294 DRLClsneEQIIIHDFILEATQDDYVleVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPTIVHDEYGAVSAGM 1371
Cdd:cd14542     81 KRVG----PDFLIRTLKVTFQKESRT--VYQFHYTAWPDHGVPSSVDpiLDLVRLVRDYQGSEDVPICVHCSAGCGRTGT 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2462591655 1372 LCAL----TTLSQQLENENaVDVFQVAKMINLMRPGVFTDIEQYQFIYK 1416
Cdd:cd14542    155 ICAIdyvwNLLKTGKIPEE-FSLFDLVREMRKQRPAMVQTKEQYELVYR 202
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
 80-360 1.86e-27

Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This vertebrate subgroup comprises isozyme V. CA V is the mitochondrial isozyme, which may play a role in gluconeogenesis and ureagenesis and possibly also in lipogenesis.


Pssm-ID: 239392  Cd Length: 236  Bit Score: 112.24  E-value: 1.86e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   80 GRHQSPIDIldqyaRVGEEYQELQLD----GFDNESSNKTWmkNTGKTVAILLKD---DYFVSGAGLPGRFKAEKVEFHW 152
Cdd:cd03118      1 GTRQSPINI-----QWRDSVYDPQLAplrvSYDPATCLYIW--NNGYSFQVEFDDstdKSGISGGPLENHYRLKQFHFHW 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  153 GHSNgSAGSEHSINGRRFPVEaedacrgdimlmlsqgmrfillglkkeqfeerkswttyqsMQIFFYNPDDFDSFQTAIS 232
Cdd:cd03118     74 GANN-EWGSEHTVDGHTYPAE----------------------------------------LHLVHWNSVKYENFEEAVM 112

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  233 ENRIIGAMAIFFQVSPRdNSALDPIIHGLKGVVHHEKETFLDPFVLRDLLPASLgSYYRYTGSLTTPPCSEIVEWIVFRR 312
Cdd:cd03118    113 EENGLAVIGVFLKLGAH-HEGLQKLVDALPEVRHKDTVVEFNPFDPSCLLPACR-DYWTYPGSLTTPPLTESVTWIIQKQ 190

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2462591655  313 PVPISYHQLEAFYSIFTTEQQDHVKsveYLRNNFRPQQRLHDRVVSKS 360
Cdd:cd03118    191 PIEVSPSQLSVFRTLLFTSRGEEEK---VMVNNFRPLQPLMNRKVRSS 235
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1182-1421 1.96e-27

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 114.26  E-value: 1.96e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1182 QKECNKEKNRNSSVVPSERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMlp 1261
Cdd:cd14604     53 EKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVM-- 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1262 dnqslAEDEFV--------YWPSR-EESMNCEAFTVTliskdrlCLSNEEQI--IIHDFILEATQDDYVLEVRHFQcpKW 1330
Cdd:cd14604    131 -----ACREFEmgrkkcerYWPLYgEEPMTFGPFRIS-------CEAEQARTdyFIRTLLLEFQNETRRLYQFHYV--NW 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1331 PNPDAPIS--STFELINVIKEEALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDI 1408
Cdd:cd14604    197 PDHDVPSSfdSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAV 276

                          250
                   ....*....|....*.
gi 2462591655 1409 ---EQYQFIYKAMLSL 1421
Cdd:cd14604    277 qtkEQYELVHRAIAQL 292
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1216-1419 3.27e-27

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 110.77  E-value: 3.27e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQS-LAEDEFVYWPsreESMNCEaftVTLISK 1293
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQlNQSnSAWPCLQYWP---EPGLQQ---YGPMEV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1294 DRLCLSNEEQIIIHDFILE--ATQDDYVLEVRHFQCPKWP----NPDAPISSTFELINVIKEEALTRDGPTIVHDEYGAV 1367
Cdd:cd14637     75 EFVSGSADEDIVTRLFRVQniTRLQEGHLMVRHFQFLRWSayrdTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGG 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462591655 1368 SAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAML 1419
Cdd:cd14637    155 RSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1216-1419 4.91e-27

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 110.14  E-value: 4.91e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQSLAEDEFV----YWPsrEESMNCEAFTVTLI 1291
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMI---TKLVEVGRVkcskYWP--DDSDTYGDIKITLL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1292 SKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPTIVHDEYGAVSA 1369
Cdd:cd14632     76 KTETLA-----EYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATglLAFIRRVKASTPPDAGPVVVHCSAGAGRT 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1370 GMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAML 1419
Cdd:cd14632    151 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
 80-357 8.45e-27

Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins (CARPs) are sequence similar to carbonic anhydrases. Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism. CARPs have lost conserved histidines involved in zinc binding and consequently their catalytic activity. CARP VIII may play roles in various biological processes of the central nervous system, and could be involved in protein-protein interactions. CARP VIII has been shown to bind inositol 1,4,5-triphosphate (IP3) receptor type I (IP3RI), reducing the affinity of the receptor for IP3. IP3RI is an intracellular IP3-gated Ca2+ channel located on intracellular Ca2+ stores. IP3RI converts IP3 signaling into Ca2+ signaling thereby participating in a variety of cell functions.


Pssm-ID: 239394  Cd Length: 256  Bit Score: 111.10  E-value: 8.45e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   80 GRHQSPIDILDQYARVGEEYQELQLdgfdneSSNKTWMK-----NTGKTVAILLKDDYFVSGAGLP--GRFKAEKVEFHW 152
Cdd:cd03120     13 GEYQSPINLNSREARYDPSLLEVRL------SPNYVVCRdceviNDGHTIQIILKSKSVLSGGPLPqgHEFELAEVRFHW 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  153 GHSNgSAGSEHSINGRRFPVEaedacrgdimlmlsqgmrfillglkkeqfeerkswttyqsMQIFFYNPDDFDSFQTAIS 232
Cdd:cd03120     87 GREN-QRGSEHTVNFKAFPME----------------------------------------LHLIHWNSTLYSSLEEAMG 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  233 ENRIIGAMAIFFQVSpRDNSALDPIIHGLKGVVHHEKETFLDPFVLRDLLP-ASLGSYYRYTGSLTTPPCSEIVEWIVFR 311
Cdd:cd03120    126 KPHGIAIIALFVQIG-KEHVGLKAVTEILQDIQYKGKSKTIPCFNPNTLLPdPLLRDYWVYEGSLTTPPCSEGVTWILFR 204

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462591655  312 RPVPISYHQLEAFYSIFTteqqdHVKSVEYLR-------NNFRPQQRLHDRVV 357
Cdd:cd03120    205 YPLTISQSQIEEFRRLRT-----HVKGAELVEgcdgllgDNFRPTQPLSDRVI 252
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1202-1419 9.42e-27

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 109.72  E-value: 9.42e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1202 RVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWPSREES 1280
Cdd:cd14631      1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKcYKYWPDDTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1281 MNceAFTVTLISKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPT 1358
Cdd:cd14631     81 YG--DFKVTCVEMEPLA-----EYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATglLSFIRRVKLSNPPSAGPI 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462591655 1359 IVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAML 1419
Cdd:cd14631    154 VVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1178-1419 9.98e-26

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 108.57  E-value: 9.98e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1178 CFSAQKECNKEKNRNSSVVPSERARVGLAplpgMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQII 1257
Cdd:cd14608     17 CRVAKLPKNKNRNRYRDVSPFDHSRIKLH----QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGV 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1258 VMLpdNQSLAEDEF---VYWPSREES---MNCEAFTVTLISKDRLCLSNEEQIIIHDFILEATQddyvlEVRHFQCPKWP 1331
Cdd:cd14608     93 VML--NRVMEKGSLkcaQYWPQKEEKemiFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETR-----EILHFHYTTWP 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1332 N---PDAPISSTFELINVIKEEALTRD-GPTIVHDEYGAVSAGMLCALTT---LSQQLENENAVDVFQVAKMINLMRPGV 1404
Cdd:cd14608    166 DfgvPESPASFLNFLFKVRESGSLSPEhGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMRKFRMGL 245

                          250
                   ....*....|....*
gi 2462591655 1405 FTDIEQYQFIYKAML 1419
Cdd:cd14608    246 IQTADQLRFSYLAVI 260
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1216-1419 1.38e-25

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 105.88  E-value: 1.38e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpDNQSLAEDEFVYWPsrEESMnceaFTVTLISKDR 1295
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVML-NEVDLAQGCPQYWP--EEGM----LRYGPIQVEC 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1296 LCLSNEEQIIIHDFI---LEATQDDYVLeVRHFQCPKWPNPDAPISSTFELINVI------KEEALTRDGPTIVHDEYGA 1366
Cdd:cd14636     74 MSCSMDCDVISRIFRicnLTRPQEGYLM-VQQFQYLGWASHREVPGSKRSFLKLIlqvekwQEECDEGEGRTIIHCLNGG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462591655 1367 VSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAML 1419
Cdd:cd14636    153 GRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVAL 205
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1216-1419 3.13e-25

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 105.06  E-value: 3.13e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqsLAE------DEfvYWPSrEESMNCEAFTVT 1289
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITN---LVEkgrrkcDQ--YWPA-DGSEEYGNFLVT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1290 LISKDRLCLSNEEQIIIHDF-ILEATQDDYVLE--VRHFQCPKWPNPDAPiSSTFELINVIKEEALTRD---GPTIVHDE 1363
Cdd:cd17668     75 QKSVQVLAYYTVRNFTLRNTkIKKGSQKGRPSGrvVTQYHYTQWPDMGVP-EYTLPVLTFVRKASYAKRhavGPVVVHCS 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591655 1364 YGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAML 1419
Cdd:cd17668    154 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1189-1416 6.30e-25

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 104.78  E-value: 6.30e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1189 KNRNSSVVPSERARVGLAPLPGmkGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQSLAE 1268
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKLKQG--DNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIML---NKLME 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1269 DE----FVYWPSREESMNC---EAFTVTLISKDRlclsnEEQIIIHDFILEATQDDYVLEVRHFQCPKWPN---PDAPIS 1338
Cdd:cd14545     76 KGqikcAQYWPQGEGNAMIfedTGLKVTLLSEED-----KSYYTVRTLELENLKTQETREVLHFHYTTWPDfgvPESPAA 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1339 STFELINVIKEEALTRD-GPTIVHDEYGAVSAGMLCALTTLSQQLENEN--AVDVFQVAKMINLMRPGVFTDIEQYQFIY 1415
Cdd:cd14545    151 FLNFLQKVRESGSLSSDvGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230


                   .
gi 2462591655 1416 K 1416
Cdd:cd14545    231 L 231
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1216-1419 7.02e-25

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 104.00  E-value: 7.02e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSlAEDEFVYWPSREESMNcEAFTVTLISKDR 1295
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDP-AQLCPQYWPENGVHRH-GPIQVEFVSADL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1296 lclsnEEQIIIHDF-ILEAT--QDDYVLeVRHFQCPKWP-NPDAPIS--STFELINVI---KEEALTRDGPTIVHDEYGA 1366
Cdd:cd14635     79 -----EEDIISRIFrIYNAArpQDGYRM-VQQFQFLGWPmYRDTPVSkrSFLKLIRQVdkwQEEYNGGEGRTVVHCLNGG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462591655 1367 VSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAML 1419
Cdd:cd14635    153 GRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1321-1420 1.77e-24

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 99.36  E-value: 1.77e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  1321 EVRHFQCPKWPNPDAPISST--FELINVIKEE--ALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENE-NAVDVFQVAK 1395
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDsiLELLRAVKKNlnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 2462591655  1396 MINLMRPGVFTDIEQYQFIYKAMLS 1420
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1321-1420 1.77e-24

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 99.36  E-value: 1.77e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  1321 EVRHFQCPKWPNPDAPISST--FELINVIKEE--ALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENE-NAVDVFQVAK 1395
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDsiLELLRAVKKNlnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 2462591655  1396 MINLMRPGVFTDIEQYQFIYKAMLS 1420
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 917-1129 1.84e-24

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 102.80  E-value: 1.84e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNL-VEKGrrkCDQYWPTENSEEYGNIIVTLKSTK 995
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  996 IHACYTVRRFSIRNtkVKKGQKGnpkgrqnERVVIQYHYTQWPDM----GVPEYALPVLTFVRRSSAARMPETGPVLVHC 1071
Cdd:cd14636     78 MDCDVISRIFRICN--LTRPQEG-------YLMVQQFQYLGWASHrevpGSKRSFLKLILQVEKWQEECDEGEGRTIIHC 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462591655 1072 SAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1129
Cdd:cd14636    149 LNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1189-1415 1.92e-24

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type tyrosine-protein phosphatase-like R (PTPRR or R-PTP-R), also called protein-tyrosine phosphatase PCPTP1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRR is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. The human and mouse PTPRR gene produces multiple neuronal protein isoforms of varying sizes (in human, PTPPBS-alpha, beta, gamma and delta). All isoforms contain the KIM motif and the catalytic PTP domain. PTPRR-deficient mice show significant defects in fine motor coordination and balance skills that are reminiscent of a mild ataxia.


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 103.46  E-value: 1.92e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1189 KNRNSSVVPSERARVGLAPL-PGMKGTDYINASYIMGYY-RSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSL 1266
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKnSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1267 AEDEFVYWPSREESMNCEAFTVTliskdrlCLSNEEQIIIHDFILEatQDDYVLEVRHFQCPKWPNPDAPISST--FELI 1344
Cdd:cd14611     82 NEKCVLYWPEKRGIYGKVEVLVN-------SVKECDNYTIRNLTLK--QGSQSRSVKHYWYTSWPDHKTPDSAQplLQLM 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462591655 1345 NVIKEEAL--TRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIY 1415
Cdd:cd14611    153 LDVEEDRLasPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1186-1419 3.41e-24

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 104.16  E-value: 3.41e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1186 NKEKNRNSSVVPSERARVGLAplpgmKGTDYINASY----IMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLp 1261
Cdd:cd14600     40 NMDKNRYKDVLPYDATRVVLQ-----GNEDYINASYvnmeIPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVML- 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1262 dnQSLAEDEFV----YWPSREESMNCEAFTVTliskdrlCLSNEEQI--IIHDFILEATQDDYVLEVRHFQCPKWPNPDA 1335
Cdd:cd14600    114 --TTLTERGRTkchqYWPDPPDVMEYGGFRVQ-------CHSEDCTIayVFREMLLTNTQTGEERTVTHLQYVAWPDHGV 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1336 PISST--FELINVIKEEALTRDgPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQF 1413
Cdd:cd14600    185 PDDSSdfLEFVNYVRSKRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKF 263


                   ....*.
gi 2462591655 1414 IYKAML 1419
Cdd:cd14600    264 VCEAIL 269
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1157-1427 4.51e-24

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 104.70  E-value: 4.51e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1157 GKTRLEkQFKLVTQCNAKYVECFsaQKECNKEKNRNSSVVPSERARVGLAPLPGmKGTDYINASYIMGYYRSNEFIITQH 1236
Cdd:PHA02747    25 GIIRDE-HHQIILKPFDGLIANF--EKPENQPKNRYWDIPCWDHNRVILDSGGG-STSDYIHANWIDGFEDDKKFIATQG 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1237 PLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE--FVYW-PSREESMNCEAFTVTLISKDRLCLSNEEQIIIHDFILEA 1313
Cdd:PHA02747   101 PFAETCADFWKAVWQEHCSIIVMLTPTKGTNGEEkcYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKD 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1314 TQddyvlEVRHFQCPKWPNPDAPISST-----FELINVIKEEALTRDG-------PTIVHDEYGAVSAGMLCALTTLSQQ 1381
Cdd:PHA02747   181 SR-----KISHFQCSEWFEDETPSDHPdfikfIKIIDINRKKSGKLFNpkdallcPIVVHCSDGVGKTGIFCAVDICLNQ 255

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2462591655 1382 LENENAVDVFQVAKMINLMRPGVFTDIEQYQFI---YKAMLSLVSTKEN 1427
Cdd:PHA02747   256 LVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIqpgYEVLHYFLSKIKA 304
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 917-1129 6.19e-24

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 101.14  E-value: 6.19e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRR-KCDQYWPTENSEEYGNIIVTLKSTK 995
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  996 IHACYTVRRFSIRN-TKVKKGQkgnpkgrqneRVVIQYHYTQW-PDMGVPEYA---LPVLTFVRRSSaaRMPETGPVLVH 1070
Cdd:cd14637     81 ADEDIVTRLFRVQNiTRLQEGH----------LMVRHFQFLRWsAYRDTPDSKkafLHLLASVEKWQ--RESGEGRTVVH 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591655 1071 CSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1129
Cdd:cd14637    149 CLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1186-1418 7.42e-24

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 104.34  E-value: 7.42e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1186 NKEKNRNSSVVPSERARVGLAPLPGMKGTD-------------------YINASYIMGYYRSNEFIITQHPLPHTTKDFW 1246
Cdd:PHA02746    51 NLKKNRFHDIPCWDHSRVVINAHESLKMFDvgdsdgkkievtsednaenYIHANFVDGFKEANKFICAQGPKEDTSEDFF 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1247 RMIWDHNAQIIVMLPDNQSLAEDEFVYWPSREESMNCEAFTVTLISKDRLCLS-NEEQIIIHDFILEATQddyvlEVRHF 1325
Cdd:PHA02746   131 KLISEHESQVIVSLTDIDDDDEKCFELWTKEEDSELAFGRFVAKILDIIEELSfTKTRLMITDKISDTSR-----EIHHF 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1326 QCPKWP---NPDAPiSSTFELINVIKEEAL----------TRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQ 1392
Cdd:PHA02746   206 WFPDWPdngIPTGM-AEFLELINKVNEEQAelikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGE 284

                          250       260
                   ....*....|....*....|....*.
gi 2462591655 1393 VAKMINLMRPGVFTDIEQYQFIYKAM 1418
Cdd:PHA02746   285 IVLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1216-1419 2.02e-23

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 99.76  E-value: 2.02e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIM-----GYYRsneFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNqslAEDEFV----YWP-SREESMNCEA 1285
Cdd:cd14538      1 YINASHIRipvggDTYH---YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQD---VEGGKVkchrYWPdSLNKPLICGG 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1286 -FTVTLISKDRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVIKE-EALTRDGPTIVHDE 1363
Cdd:cd14538     75 rLEVSLEKYQSL-----QDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTP-QSADPLLRFIRYmRRIHNSGPIVVHCS 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591655 1364 YGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAML 1419
Cdd:cd14538    149 AGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACL 204
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1186-1418 2.29e-23

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 101.00  E-value: 2.29e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1186 NKEKNRNSSVVPSERARVGLAPL-PGMKGTDYINASYIM-----GYYRSNE--FIITQHPLPHTTKDFWRMIWDHNAQII 1257
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRdPNVPGSDYINANYIRnenegPTTDENAktYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1258 VMLPDNQSLAEDEFV-YWPsreESMNCEAFtvtliskDRLCLSNEEQIIIHDFIL------EATQDDYVLEVRHFQCPKW 1330
Cdd:cd14544     81 VMTTKEVERGKNKCVrYWP---DEGMQKQY-------GPYRVQNVSEHDTTDYTLrelqvsKLDQGDPIREIWHYQYLSW 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1331 PN---PDAP--ISSTFELINViKEEALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENEN---AVDVFQVAKMINLMRP 1402
Cdd:cd14544    151 PDhgvPSDPggVLNFLEDVNQ-RQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRS 229

                          250
                   ....*....|....*.
gi 2462591655 1403 GVFTDIEQYQFIYKAM 1418
Cdd:cd14544    230 GMVQTEAQYKFIYVAV 245
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1215-1420 3.38e-23

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 99.33  E-value: 3.38e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1215 DYINASYI-MGYYRS---NEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQSLAEDEFV----YWPSREESMNCEAF 1286
Cdd:cd14541      1 DYINANYVnMEIPGSgivNRYIAAQGPLPNTCADFWQMVWEQKSTLIVML---TTLVERGRVkchqYWPDLGETMQFGNL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1287 TVTliskdrlCLSNEEQI--IIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTfELINVIKEEALTRDG---PTIVH 1361
Cdd:cd14541     78 QIT-------CVSEEVTPsfAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSS-DFLDFVKRVRQNRVGmvePTVVH 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591655 1362 DEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAMLS 1420
Cdd:cd14541    150 CSAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILR 208
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 917-1128 3.87e-23

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 98.91  E-value: 3.87e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCdQYWPteNSEEYGN---IIVTLKS 993
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWP--NKDEPINcetFKVTLIA 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  994 TKiHACYT------VRRFSIRNTkvkkgqkgnpkgrQNERVVIQYHYT--QWPDMGVP-EYALPVLTFVRRSSAARmpeT 1064
Cdd:cd17669     78 EE-HKCLSneekliIQDFILEAT-------------QDDYVLEVRHFQcpKWPNPDSPiSKTFELISIIKEEAANR---D 140

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462591655 1065 GPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALL 1128
Cdd:cd17669    141 GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PHA02738 PHA02738
hypothetical protein; Provisional
 1179-1418 5.83e-23

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 101.54  E-value: 5.83e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1179 FSAQKEcNKEKNRNSSVVPSERARVGLaPLPGMKGtDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIV 1258
Cdd:PHA02738    43 FNAEKK-NRKLNRYLDAVCFDHSRVIL-PAERNRG-DYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIV 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1259 ML-PDNQSLAEDEFVYWPSREE-SMNCEAFTVTLISKDRLCLSNEEQIIIHDFIlEATQddyvlEVRHFQCPKWPNPDAP 1336
Cdd:PHA02738   120 MLcKKKENGREKCFPYWSDVEQgSIRFGKFKITTTQVETHPHYVKSTLLLTDGT-SATQ-----TVTHFNFTAWPDHDVP 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1337 iSSTFELINVI----------KEEAL------TRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLM 1400
Cdd:PHA02738   194 -KNTSEFLNFVlevrqcqkelAQESLqighnrLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQ 272

                          250
                   ....*....|....*...
gi 2462591655 1401 RPGVFTDIEQYQFIYKAM 1418
Cdd:PHA02738   273 RYYSLFIPFQYFFCYRAV 290
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1186-1419 3.18e-22

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 97.21  E-value: 3.18e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1186 NKEKNRNSSVVPSERARVGLaplpGMKGtDYINASYIMGYYRSNEF--IITQHPLPHTTKDFWRMIWDHNAQIIVMLPDN 1263
Cdd:cd14597      3 NRKKNRYKNILPYDTTRVPL----GDEG-GYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1264 qslAEDEFV----YWPsreesmncEAFTVTLISKDRLCLS-----NEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPD 1334
Cdd:cd14597     78 ---VEGGKIkcqrYWP--------EILGKTTMVDNRLQLTlvrmqQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHD 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1335 APiSSTFELINVIK-EEALTRDGPTIVHDEYGAVSAGML-C---ALTTLSQQLEnenaVDVFQVAKMINLMRPGVFTDIE 1409
Cdd:cd14597    147 TP-SQPEQLLTFISyMRHIHKSGPIITHCSAGIGRSGTLiCidvVLGLISKDLD----FDISDIVRTMRLQRHGMVQTED 221

                          250
                   ....*....|
gi 2462591655 1410 QYQFIYKAML 1419
Cdd:cd14597    222 QYIFCYQVIL 231
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1186-1422 4.83e-22

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 98.15  E-value: 4.83e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1186 NKEKNRNSSVVPSERARVGLAPLPgMKGTDYINASYIMGYYRSNE--FIITQHPLPHTTKDFWRMIWDHNAQIIVMLPdn 1263
Cdd:cd14599     38 NAERNRIREVVPYEENRVELVPTK-ENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVT-- 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1264 qslAEDE------FVYWP---SREESMNCEAFTVTL-ISKDRLCLSNEEQIIIHdfiLEATQDDYVLevrHFQCPKWPNP 1333
Cdd:cd14599    115 ---AEEEggrsksHRYWPklgSKHSSATYGKFKVTTkFRTDSGCYATTGLKVKH---LLSGQERTVW---HLQYTDWPDH 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1334 DAP------------ISSTFELINVIKEEALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMR 1401
Cdd:cd14599    186 GCPeevqgflsyleeIQSVRRHTNSMLDSTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQR 265

                          250       260
                   ....*....|....*....|.
gi 2462591655 1402 PGVFTDIEQYQFIYKAMLSLV 1422
Cdd:cd14599    266 MFMIQTIAQYKFVYQVLIQFL 286
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1182-1424 5.98e-22

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 97.26  E-value: 5.98e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1182 QKECNKEKNRNSSVVPSERARVGLAPL-PGMKGTDYINASYIMGYYRSNE-----FIITQHPLPHTTKDFWRMIWDHNAQ 1255
Cdd:cd14606     14 QRPENKSKNRYKNILPFDHSRVILQGRdSNIPGSDYINANYVKNQLLGPDenaktYIASQGCLEATVNDFWQMAWQENSR 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1256 IIVMLPDNQSLAEDEFV-YWPSREESMNCEAFTVTLIS-------KDR-LCLSneeqiIIHDfileatqDDYVLEVRHFQ 1326
Cdd:cd14606     94 VIVMTTREVEKGRNKCVpYWPEVGMQRAYGPYSVTNCGehdtteyKLRtLQVS-----PLDN-------GELIREIWHYQ 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1327 CPKWPNPDAP-----ISSTFELINViKEEALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENA---VDVFQVAKMIN 1398
Cdd:cd14606    162 YLSWPDHGVPsepggVLSFLDQINQ-RQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVR 240

                          250       260
                   ....*....|....*....|....*.
gi 2462591655 1399 LMRPGVFTDIEQYQFIYKAMLSLVST 1424
Cdd:cd14606    241 AQRSGMVQTEAQYKFIYVAIAQFIET 266
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 917-1128 6.18e-22

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 95.52  E-value: 6.18e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITN---LVEkgrrkcDQ--YWPT-ENSEEYGNIIVT 990
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqgLAE------DEfvYWPSrEESMNCEAFTVT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  991 LKSTKihacytvrRFSIRNTKVKKGQKGNPKGRQNERVVIQYHYT--QWPDMGVPEYALPVLTFVRRSSAarMPETGPVL 1068
Cdd:cd17670     75 LISKD--------RLCLSNEEQIIIHDFILEATQDDYVLEVRHFQcpKWPNPDAPISSTFELINVIKEEA--LTRDGPTI 144

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1069 VHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALL 1128
Cdd:cd17670    145 VHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 917-1129 8.15e-22

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 95.14  E-value: 8.15e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  917 YINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLveKGRRKCDQYWPTENSEEYGNIIVTLKSTKI 996
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSADL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  997 HACYTVRRFSIRNTKvkkgqkgnpKGRQNERVVIQYHYTQWPDM-GVPEYALPVLTFVRRSSAARMPE---TGPVLVHCS 1072
Cdd:cd14635     79 EEDIISRIFRIYNAA---------RPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYnggEGRTVVHCL 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462591655 1073 AGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 1129
Cdd:cd14635    150 NGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1216-1416 1.13e-21

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 94.76  E-value: 1.13e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYR-SNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFV-YWPS-REESMNCEAFTVTLIS 1292
Cdd:cd14539      1 YINASLIEDLTPyCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHrYWPTeRGQALVYGAITVSLQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1293 KDRLCLSNEEQIII--HDFILEATqddyvleVRHFQCPKWP---NPDAPiSSTFELINVIKEEALTRDG---PTIVHDEY 1364
Cdd:cd14539     81 VRTTPTHVERIISIqhKDTRLSRS-------VVHLQFTTWPelgLPDSP-NPLLRFIEEVHSHYLQQRSlqtPIVVHCSS 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462591655 1365 GAVSAGMLCALTTLSQQLENENAV-DVFQVAKMINLMRPGVFTDIEQYQFIYK 1416
Cdd:cd14539    153 GVGRTGAFCLLYAAVQEIEAGNGIpDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1216-1416 2.15e-21

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 93.74  E-value: 2.15e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWPSREESMNCEAFTVTLISKD 1294
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKcAQYWPSMEEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1295 RLClsnEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTR--DGPTIVHDEYGAVSAGML 1372
Cdd:cd14557     81 KIC---PDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNffSGPIVVHCSAGVGRTGTY 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2462591655 1373 CALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYK 1416
Cdd:cd14557    158 IGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1186-1424 2.92e-21

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 95.08  E-value: 2.92e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1186 NKEKNRNSSVVPSERARVGLAP-LPGMKGTDYINASYIMGYYRSN--------EFIITQHPLPHTTKDFWRMIWDHNAQI 1256
Cdd:cd14605      2 NKNKNRYKNILPFDHTRVVLHDgDPNEPVSDYINANIIMPEFETKcnnskpkkSYIATQGCLQNTVNDFWRMVFQENSRV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1257 IVMLPDNQSLAEDEFV-YWPsreESMNCEAFTVTLIskdrlclSNEEQIIIHDFIL------EATQDDYVLEVRHFQCPK 1329
Cdd:cd14605     82 IVMTTKEVERGKSKCVkYWP---DEYALKEYGVMRV-------RNVKESAAHDYILrelklsKVGQGNTERTVWQYHFRT 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1330 WPNPDAP-----ISSTFELINvIKEEALTRDGPTIVHDEYGAVSAGMLCALTTLSQQLENENA---VDVFQVAKMINLMR 1401
Cdd:cd14605    152 WPDHGVPsdpggVLDFLEEVH-HKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQR 230

                          250       260
                   ....*....|....*....|...
gi 2462591655 1402 PGVFTDIEQYQFIYKAMLSLVST 1424
Cdd:cd14605    231 SGMVQTEAQYRFIYMAVQHYIET 253
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1216-1416 3.45e-21

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 93.05  E-value: 3.45e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFV-YWPSReesmNCEAFtvtliSKD 1294
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSqYWPDQ----GCWTY-----GNL 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1295 RLCLSNEEQIIIH---DFILEATQDDY----VLEVRHFQCPKWPN---PDAPIsSTFELINVIKEEALTRDGPTIVHDEY 1364
Cdd:cd14551     72 RVRVEDTVVLVDYttrKFCIQKVNRGIgekrVRLVTQFHFTSWPDfgvPFTPI-GMLKFLKKVKSANPPRAGPIVVHCSA 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462591655 1365 GAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYK 1416
Cdd:cd14551    151 GVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1173-1418 1.62e-20

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 92.72  E-value: 1.62e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1173 AKYVEcfsaqkecNKEKNRNSSVVPSERARVGLAPLPgmkgTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDH 1252
Cdd:cd14607     19 AKYPE--------NRNRNRYRDVSPYDHSRVKLQNTE----NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQ 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1253 NAQIIVMLpdnQSLAEDEFV----YWPSREESM---NCEAFTVTLISKDRlclsnEEQIIIHDFILEATQDDYVLEVRHF 1325
Cdd:cd14607     87 KTKAVVML---NRIVEKDSVkcaqYWPTDEEEVlsfKETGFSVKLLSEDV-----KSYYTVHLLQLENINSGETRTISHF 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1326 QCPKWPN---PDAPISSTFELINVIKEEALTRD-GPTIVHDEYGAVSAGMLCALTTLSQQLENEN--AVDVFQVAKMINL 1399
Cdd:cd14607    159 HYTTWPDfgvPESPASFLNFLFKVRESGSLSPEhGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRK 238

                          250
                   ....*....|....*....
gi 2462591655 1400 MRPGVFTDIEQYQFIYKAM 1418
Cdd:cd14607    239 YRMGLIQTPDQLRFSYMAV 257
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1216-1419 5.13e-20

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 89.81  E-value: 5.13e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYRSNE--FIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWP-SREESMNCEAFTVTLI 1291
Cdd:cd14596      1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKcHRYWPeTLQEPMELENYQLRLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1292 SKDRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTfELINVIK-EEALTRDGPTIVHDEYGAVSAG 1370
Cdd:cd14596     81 NYQAL-----QYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSD-QLVKFICyMRKVHNTGPIVVHCSAGIGRAG 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2462591655 1371 MLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAML 1419
Cdd:cd14596    155 VLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVL 203
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1216-1417 6.40e-20

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 89.81  E-value: 6.40e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYY-RSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFV-YWPsrEESMNC-EAFTVTLIS 1292
Cdd:cd14546      1 YINASTIYDHDpRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCArYWP--EEGSEVyHIYEVHLVS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1293 KDRLClsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPTIVHDEYGAVSAG 1370
Cdd:cd14546     79 EHIWC----DDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKplLEFRRKVNKSYRGRSCPIVVHCSDGAGRTG 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2462591655 1371 MLCAL-TTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKA 1417
Cdd:cd14546    155 TYILIdMVLNRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTA 202
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1216-1419 1.57e-19

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 89.05  E-value: 1.57e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYRSNE--FIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLA-EDEFVYWP---SREESMNCEAFTVT 1289
Cdd:cd14540      1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGrEKCFRYWPtlgGEHDALTFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1290 L-ISKDRLCLsneeqiIIHDFILEATQDDYVLEVRHFQCPKWPN---PDAPIS--STFELINVIKEEAL------TRDGP 1357
Cdd:cd14540     81 TkFSVSSGCY------TTTGLRVKHTLSGQSRTVWHLQYTDWPDhgcPEDVSGflDFLEEINSVRRHTNqdvaghNRNPP 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462591655 1358 TIVHDEYGAVSAG--MLCALttLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAML 1419
Cdd:cd14540    155 TLVHCSAGVGRTGvvILADL--MLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLI 216
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1161-1425 8.95e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 88.91  E-value: 8.95e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1161 LEKQFKLVTQCNAKYvECFSAQKECNKEKNRNSSVVPSERARVGLAPLPGmkGTDYINASYIMGYYRSNEFIITQHPLPH 1240
Cdd:PHA02742    28 LKEEHEHIMQEIVAF-SCNESLELKNMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKGRFICTQAPLEE 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1241 TTKDFWRMIWDHNAQIIVMLP----DNQslaEDEFVYWPSREESMNCEA-FTV-TLISKD-------RLCLSNeeqiiih 1307
Cdd:PHA02742   105 TALDFWQAIFQDQVRVIVMITkimeDGK---EACYPYWMPHERGKATHGeFKIkTKKIKSfrnyavtNLCLTD------- 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1308 dfileaTQDDYVLEVRHFQCPKWPNPDAP--ISSTFELINVIKEEALTRD-----------GPTIVHDEYGAVSAGMLCA 1374
Cdd:PHA02742   175 ------TNTGASLDIKHFAYEDWPHGGLPrdPNKFLDFVLAVREADLKADvdikgenivkePPILVHCSAGLDRAGAFCA 248

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462591655 1375 LtTLSQQLENENA-VDVFQVAKMINLMRPGVFTDIEQYQFIYKAML---SLVSTK 1425
Cdd:PHA02742   249 I-DICISKYNERAiIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLifaKLMADK 302
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 880-1127 1.38e-17

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 85.02  E-value: 1.38e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  880 SNHPENKHK--NRYINILAYDHSRVKLRplpgKDSKhsdYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGI 957
Cdd:PHA02740    46 CAQAENKAKdeNLALHITRLLHRRIKLF----NDEK---VLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQI 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  958 IVMITNLVEKgrrKC-DQYWPTENS--EEYGNI-IVTLK-STKIHACYTVrrFSIRNtkvKKGQkgnpkgrqnERVVIQY 1032
Cdd:PHA02740   119 IVLISRHADK---KCfNQFWSLKEGcvITSDKFqIETLEiIIKPHFNLTL--LSLTD---KFGQ---------AQKISHF 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1033 HYTQWPDMGVPEYALPVLTF----------VRRSSAARmpETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGF 1102
Cdd:PHA02740   182 QYTAWPADGFSHDPDAFIDFfcniddlcadLEKHKADG--KIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANA 259

                          250       260
                   ....*....|....*....|....*
gi 2462591655 1103 LKHIRTQRNYLVQTEEQYIFIHDAL 1127
Cdd:PHA02740   260 LKKVRQKKYGCMNCLDDYVFCYHLI 284
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1215-1419 6.70e-17

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 81.14  E-value: 6.70e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1215 DYINASYIMGYYRS----NEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDE-FVYWPSREESMNCEAFTVT 1289
Cdd:cd14601      1 DYINANYINMEIPSssiiNRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKcHQYWPEPSGSSSYGGFQVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1290 liskdrlCLSNE--EQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPTIVHDEYG 1365
Cdd:cd14601     81 -------CHSEEgnPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSdfLDFVCLVRNKRAGKDEPVVVHCSAG 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462591655 1366 AVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAML 1419
Cdd:cd14601    154 IGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAIL 207
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1216-1422 9.61e-17

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 80.79  E-value: 9.61e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYRSNE--FIITQHPLPHTTKDFWRMIWDHNAQIIVMLP-DNQSLAEDEFVYWP---SREESMNCEAFTVT 1289
Cdd:cd14598      1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTaEEEGGREKSFRYWPrlgSRHNTVTYGRFKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1290 L-ISKDRLCLSNEEQIIIHdfiLEATQDDYVLevrHFQCPKWPNPDAP------ISSTFELINVIKEEALTRD-----GP 1357
Cdd:cd14598     81 TrFRTDSGCYATTGLKIKH---LLTGQERTVW---HLQYTDWPEHGCPedlkgfLSYLEEIQSVRRHTNSTIDpkspnPP 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462591655 1358 TIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAMLSLV 1422
Cdd:cd14598    155 VLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1216-1415 6.42e-16

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 77.89  E-value: 6.42e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1216 YINASYIMGYYRSN--EFIITQHPLPHTTKDFWRMIWDHNAQIIVMLP---DNQSLAEDEFVYWPSREESMNCEAFTVTL 1290
Cdd:cd17658      1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTrlvDNYSTAKCADYFPAEENESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1291 ISkdrlcLSNEEQIIIHDFiLEATQ---DDYVLEVRHFQCPKWPNPDAPiSSTFELINVIKEEALTRD--GPTIVHDEYG 1365
Cdd:cd17658     81 KK-----LKHSQHSITLRV-LEVQYiesEEPPLSVLHIQYPEWPDHGVP-KDTRSVRELLKRLYGIPPsaGPIVVHCSAG 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462591655 1366 AVSAGMLCAL-TTLSQQLENE-NAVDVFQVAKMINLMRPGVFTDIEQYQFIY 1415
Cdd:cd17658    154 IGRTGAYCTIhNTIRRILEGDmSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 889-1129 9.89e-13

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 69.35  E-value: 9.89e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  889 NRYINIlaydHSRVKLrpLPGKDskhsdyINANYVDGYNKAKAyIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKG 968
Cdd:cd14559      1 NRFTNI----QTRVST--PVGKN------LNANRVQIGNKNVA-IACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQ 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  969 RRKCDQYWptENSEEYGNIIVtlKSTKIHACYTVRRFSIR--NTKVKKGQKGNPkgrqnervVIQYHYTQWPDMG-VPEY 1045
Cdd:cd14559     68 RKGLPPYF--RQSGTYGSVTV--KSKKTGKDELVDGLKADmyNLKITDGNKTIT--------IPVVHVTNWPDHTaISSE 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1046 ALPVLT--------------FVRRSSAARMPETGPVLVHCSAGVGRTGTYIvidSMLQQIKDKSTVNVLGFLKHIRTQRN 1111
Cdd:cd14559    136 GLKELAdlvnksaeekrnfyKSKGSSAINDKNKLLPVIHCRAGVGRTGQLA---AAMELNKSPNNLSVEDIVSDMRTSRN 212

                          250
                   ....*....|....*....
gi 2462591655 1112 -YLVQTEEQYifihDALLE 1129
Cdd:cd14559    213 gKMVQKDEQL----DTLKE 227
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1217-1425 6.98e-11

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 64.99  E-value: 6.98e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1217 INASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQSLAEDE--FVYWPSREEsmnceaftvTLISKD 1294
Cdd:PHA02740    79 LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLI---SRHADKKcfNQFWSLKEG---------CVITSD 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1295 RLCLSNEEQIIIHDFILE----ATQDDYVLEVRHFQCPKWP------NPDAPISSTFEL----INVIKEEALTRDGPTIV 1360
Cdd:PHA02740   147 KFQIETLEIIIKPHFNLTllslTDKFGQAQKISHFQYTAWPadgfshDPDAFIDFFCNIddlcADLEKHKADGKIAPIII 226

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462591655 1361 HDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFIYKAMLSLVSTK 1425
Cdd:PHA02740   227 DCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLKEK 291
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 388-478 3.83e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 55.20  E-value: 3.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  388 SPPIHMKVQPLNQTALQVSWSQPETIyHPPIMNYMISYSWTKNEDEKEktFTKDSDKDLKATISHVSPDSLYLFRVQAVc 467
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPEDD-GGPITGYVVEYREKGSGDWKE--VEVTPGSETSYTLTGLKPGTEYEFRVRAV- 77

                           90
                   ....*....|.
gi 2462591655  468 RNDMRSDFSQT 478
Cdd:cd00063     78 NGGGESPPSES 88
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1030-1125 4.15e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 56.52  E-value: 4.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1030 IQYHYTQWPDMGVPEYA--LPVLTFVRRssaaRMPETGPVLVHCSAGVGRTGT----YIVIDSM-LQQIkdkstvnvlgf 1102
Cdd:COG2453     48 LEYLHLPIPDFGAPDDEqlQEAVDFIDE----ALREGKKVLVHCRGGIGRTGTvaaaYLVLLGLsAEEA----------- 112

                           90       100
                   ....*....|....*....|...
gi 2462591655 1103 LKHIRTQRNYLVQTEEQYIFIHD 1125
Cdd:COG2453    113 LARVRAARPGAVETPAQRAFLER 135
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 388-466 5.67e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 54.54  E-value: 5.67e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591655   388 SPPIHMKVQPLNQTALQVSWSQPEtiyHPPIMNYMISYSWTKNEDEKEKTFTKDSDKDLKATISHVSPDSLYLFRVQAV 466
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
PLN02179 PLN02179
carbonic anhydrase
 17-312 2.62e-08

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 56.14  E-value: 2.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   17 TSSVLHYVVCFPALTEGYVGALHENRHGSA--VQIRRRKASGDPYWaysGAYGPeHWvtsSVSCGGRHQSPIDILDQyaR 94
Cdd:PLN02179     5 TKTIFFFVVFFIDLFFPNILLVYAREIGNKplFTYKQKTEKGPAEW---GKLNP-QW---KVCSTGKYQSPIDLTDE--R 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655   95 VGEEYqelqldgfdnessNKTWMKNTGKTVAILLK--DDYFVSGAGLPGRFKAEKVEF-----HWgHSNgsagSEHSING 167
Cdd:PLN02179    76 VSLIH-------------DQALSRHYKPAPAVIQSrgHDVMVSWKGDAGKITIHQTDYklvqcHW-HSP----SEHTING 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  168 RRFPVEAEdacrgdiMLMLSQGMRFILLGLKKEQFEerkswttyqsmqiffynPDDFdsfqtaisenriigamaiffqvs 247
Cdd:PLN02179   138 TSYDLELH-------MVHTSASGKTAVVGVLYKLGE-----------------PDEF----------------------- 170

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591655  248 prdnsaLDPIIHGLKGVVHHEKET-FLDPFVLRdllpASLGSYYRYTGSLTTPPCSEIVEWIVFRR 312
Cdd:PLN02179   171 ------LTKLLNGIKGVGKKEINLgIVDPRDIR----FETNNFYRYIGSLTIPPCTEGVIWTVVKR 226
fn3 pfam00041
Fibronectin type III domain;
388-466 3.65e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 52.03  E-value: 3.65e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591655  388 SPPIHMKVQPLNQTALQVSWSQPETiYHPPIMNYMISYsWTKNEDEKEKTFTKDSDKDlKATISHVSPDSLYLFRVQAV 466
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPD-GNGPITGYEVEY-RPKNSGEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAV 76
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1065-1125 8.46e-07

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 49.27  E-value: 8.46e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462591655 1065 GPVLVHCSAGVGRTGTYIVIDSMLQQIKDkstvnVLGFLKHIRTQR-NYLVQTEEQYIFIHD 1125
Cdd:cd14494     57 EPVLVHCKAGVGRTGTLVACYLVLLGGMS-----AEEAVRIVRLIRpGGIPQTIEQLDFLIK 113
PLN02202 PLN02202
carbonate dehydratase
 289-357 2.74e-06

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 50.83  E-value: 2.74e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591655  289 YYRYTGSLTTPPCSEIVEWIVFRRPVPISYHQLEAFYSIFTTEqqdhvksveyLRNNFRPQQRLHDRVV 357
Cdd:PLN02202   204 YFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLRSPLDKS----------FKNNSRPCQPLNGRRV 262
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1030-1125 2.87e-06

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia.


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 49.65  E-value: 2.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1030 IQYHYTQWPDMGVPEYALpVLTFVRRSSAArMPETGPVLVHCSAGVGRTGtyIVIDSMLQQIKDKSTVNVLGFlkhIRTQ 1109
Cdd:cd14506     77 IYFYNFGWKDYGVPSLTT-ILDIVKVMAFA-LQEGGKVAVHCHAGLGRTG--VLIACYLVYALRMSADQAIRL---VRSK 149

                           90
                   ....*....|....*.
gi 2462591655 1110 RNYLVQTEEQYIFIHD 1125
Cdd:cd14506    150 RPNSIQTRGQVLCVRE 165
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1030-1125 3.75e-06

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 48.41  E-value: 3.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1030 IQYHYTQWPDMGVP---EYALPVLTFVRrsSAARMPETgpVLVHCSAGVGRTGTyiVIDSMLQQIKDKSTVNVLgfLKHI 1106
Cdd:cd14505     73 ITWHHLPIPDGGVPsdiAQWQELLEELL--SALENGKK--VLIHCKGGLGRTGL--IAACLLLELGDTLDPEQA--IAAV 144

                           90
                   ....*....|....*....
gi 2462591655 1107 RTQRNYLVQTEEQYIFIHD 1125
Cdd:cd14505    145 RALRPGAIQTPKQENFLHQ 163
PHA03169 PHA03169
hypothetical protein; Provisional
 584-742 7.88e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 49.97  E-value: 7.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  584 ASKQAARPVLATTealASPGPDGDSSPtkDGEGTEEGEKDEKSESEDGEREHEEDGEKDSEKKEKSGVTHAAEERNQtEP 663
Cdd:PHA03169   105 PSPSGSAEELASG---LSPENTSGSSP--ESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPE-EP 178

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591655  664 SPTPSSPNRTAEGGHQTIPGHEQDHTAVPTDQTGgrRDAGPGldPDMVTSTQVPPTATEEQYAgSDPKRPEMPSKKPMS 742
Cdd:PHA03169   179 EPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPG--EPQSPT--PQQAPSPNTQQAVEHEDEP-TEPEREGPPFPGHRS 252
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1030-1123 1.64e-04

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 43.42  E-value: 1.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1030 IQYHYTQWPDMGVP--EYALPVLTFVRRSSAarmpETGPVLVHCSAGVGRTGT----YIVIDSMLQQIKDkstvnvlgfL 1103
Cdd:cd14504     50 LRYHHIPIEDYTPPtlEQIDEFLDIVEEANA----KNEAVLVHCLAGKGRTGTmlacYLVKTGKISAVDA---------I 116

                           90       100
                   ....*....|....*....|
gi 2462591655 1104 KHIRTQRNYLVQTEEQYIFI 1123
Cdd:cd14504    117 NEIRRIRPGSIETSEQEKFV 136
PHA03169 PHA03169
hypothetical protein; Provisional
 600-683 4.02e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 44.58  E-value: 4.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  600 ASPGPDGDSSPTKDGEGTEEGEkdEKSESEDGEREHEEDGEKDSEKKEK----------SGVTHAAEERNQTEPSPTPSS 669
Cdd:PHA03169   175 PEEPEPPTSEPEPDSPGPPQSE--TPTSSPPPQSPPDEPGEPQSPTPQQapspntqqavEHEDEPTEPEREGPPFPGHRS 252

                           90
                   ....*....|....*
gi 2462591655  670 PNRTAEG-GHQTIPG 683
Cdd:PHA03169   253 HSYTVVGwKPSTRPG 267
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
1065-1107 7.15e-04

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 41.50  E-value: 7.15e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 2462591655  1065 GPVLVHCSAGVGRTGTYIVidSMLQQIKDKSTVNVLGFLKHIR 1107
Cdd:smart00195   79 GKVLVHCQAGVSRSATLII--AYLMKTRNMSLNDAYDFVKDRR 119
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 567-774 7.46e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.39  E-value: 7.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  567 SSFPSTVWPTRLPTAASASKQAARPVLATTEALASPGPDGDSSPTK-DGEGTEEGEKDEKSESEDGEREHEEDGEKDsek 645
Cdd:PHA03307   151 SPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPStPPAAASPRPPRRSSPISASASSPAPAPGRS--- 227

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655  646 keksgvthAAEERNQTEPSPTPSSPNRTAEGGHQTIPGHEQDHTAVPTDQTGGRRDAGPGLDPdmvtSTQVPPTATEEQY 725
Cdd:PHA03307   228 --------AADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRP----GPASSSSSPRERS 295

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2462591655  726 AGSDPKRPEMPSKKPMSRGDRFSEDSRfiTVNPAEKNTSGMISRPAPGR 774
Cdd:PHA03307   296 PSPSPSSPGSGPAPSSPRASSSSSSSR--ESSSSSTSSSSESSRGAAVS 342
PTPLP-like cd14495
Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ...
 1021-1114 2.68e-03

Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily contains the tandem protein tyrosine phosphatase (PTP)-like domains of protein tyrosine phosphatase-like phytases (PTPLPs) and similar domains including the PTP domain of Pseudomonas syringae tyrosine-protein phosphatase hopPtoD2. PTPLPs, also known as cysteine phytases, are one of four known classes of phytases, enzymes that degrade phytate (inositol hexakisphosphate [InsP(6)]) to less-phosphorylated myo-inositol derivatives. Phytate is the most abundant cellular inositol phosphate and plays important roles in a broad scope of cellular processes, including DNA repair, RNA processing and export, development, apoptosis, and pathogenicity. PTPLPs adopt a PTP fold, including the active-site signature sequence (CX5R(S/T)) and utilize a classical PTP reaction mechanism. However, these enzymes display no catalytic activity against classical PTP substrates due to several unique structural features that confer specificity for myo-inositol polyphosphates.


Pssm-ID: 350345  Cd Length: 278  Bit Score: 41.59  E-value: 2.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591655 1021 KGRQNERVVIQYHytQWPDmgvPEYALPVLTFVRRssaarMPETGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKStvnvl 1100
Cdd:cd14495    153 KGAHYVRIAATDH--VWPD---DEEIDAFVAFYRS-----LPADAWLHFHCRAGKGRTTTFMVMYDMLKNPKDVS----- 217

                           90
                   ....*....|....
gi 2462591655 1101 gfLKHIrTQRNYLV 1114
Cdd:cd14495    218 --FDDI-IARQYLI 228
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 1063-1082 9.53e-03

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 38.59  E-value: 9.53e-03
                           10        20
                   ....*....|....*....|
gi 2462591655 1063 ETGPVLVHCSAGVGRTGTYI 1082
Cdd:cd14499    108 EKGAIAVHCKAGLGRTGTLI 127
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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